http://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&feed=atom&action=historyTeam:ITB Indonesia/Parts - Revision history2024-03-28T17:09:01ZRevision history for this page on the wikiMediaWiki 1.16.5http://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=387095&oldid=prevErawijantari at 02:11, 18 October 20142014-10-18T02:11:52Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p align="justify">Improvisation the part submitted by UC Davis team <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p align="justify">Improvisation the part submitted by UC Davis team <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;"></ol></ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p><del class="diffchange diffchange-inline">1Georgiou</del>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. <i> Protein Engineering, 9, 239-247</i>.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>><ins class="diffchange diffchange-inline">Georgiou</ins>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. <i> Protein Engineering, 9, 239-247</i>.</p></div></td></tr>
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</table>Erawijantarihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=386253&oldid=prevErawijantari at 02:03, 18 October 20142014-10-18T02:03:58Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p align="justify">The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">(<del class="diffchange diffchange-inline">Bba_K!387001</del>)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p align="justify">The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">(<ins class="diffchange diffchange-inline">Bba_K1387001</ins>)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td></tr>
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</table>Erawijantarihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=318412&oldid=prevErawijantari at 12:21, 17 October 20142014-10-17T12:21:31Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">(Bba_K!387001)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>>The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">(Bba_K!387001)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The casette of degradation module <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387006">(BBa_K1387006) </a> is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>>The casette of degradation module <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387006">(BBa_K1387006) </a> is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, make a new part called </p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, make a new part called <ins class="diffchange diffchange-inline"> <a style="color:#342D7E" href="http://parts.igem.org/Part:Bba_K1387005"> Bba_K1387005 </a> </ins></p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>This casette <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_K1387002)</a> consist of TetR <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_C0040">(BBa_C0040)</a> and Double Terminator <a style="color:#342D7E"href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>>This casette <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_K1387002)</a> consist of TetR <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_C0040">(BBa_C0040)</a> and Double Terminator <a style="color:#342D7E"href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. <a style="color:#342D7E"href="hhttp://parts.igem.org/Part:BBa_K1387000"> BBa_K1387000 </a> consist of RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a> and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>, while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">BBa_K1387001 </a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. <a style="color:#342D7E"href="hhttp://parts.igem.org/Part:BBa_K1387000"> BBa_K1387000 </a> consist of RBS <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a> and double terminator <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>, while the complete module was contained in <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K1387001">BBa_K1387001 </a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p <ins class="diffchange diffchange-inline">align="justify"</ins>>Improvisation the part submitted by UC Davis team <a style="color:#342D7E" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. <i> Protein Engineering, 9, 239-247</i>.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. <i> Protein Engineering, 9, 239-247</i>.</p></div></td></tr>
</table>Erawijantarihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=301444&oldid=prevErawijantari at 03:38, 17 October 20142014-10-17T03:38:52Z<p></p>
<table style="background-color: white; color:black;">
<col class='diff-marker' />
<col class='diff-content' />
<col class='diff-marker' />
<col class='diff-content' />
<tr valign='top'>
<td colspan='2' style="background-color: white; color:black;">← Older revision</td>
<td colspan='2' style="background-color: white; color:black;">Revision as of 03:38, 17 October 2014</td>
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<td colspan="2" class="diff-lineno">Line 238:</td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K1387001">(Bba_K!387001)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>, RBS <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. BBa_K1387000 consist of RBS (Bba_B0034), amilCP (BBa_K592025) and double terminator (BBa_B0015), while the complete module was contained in <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K1387001">(Bba_K!387001)</a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The casette of degradation module <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K1387006">(BBa_K1387006) </a> is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The casette of degradation module <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K1387006">(BBa_K1387006) </a> is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, make a new part called </p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, make a new part called </p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>This casette <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_K1387002)</a> consist of TetR <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_C0040">(BBa_C0040)</a> and Double Terminator <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>This casette <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_K1387002)</a> consist of TetR <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_C0040">(BBa_C0040)</a> and Double Terminator <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>"href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a><del class="diffchange diffchange-inline">(, </del>RBS <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. <a style="<del class="diffchange diffchange-inline">blue</del>" href="hhttp://parts.igem.org/Part:BBa_K1387000"> BBa_K1387000 </a> consist of RBS <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a> and double terminator <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>, while the complete module was contained in <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K1387001">BBa_K1387001 </a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K339010">(BBa_K339010)</a>RBS <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a>, and double terminator <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>. <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>"href="hhttp://parts.igem.org/Part:BBa_K1387000"> BBa_K1387000 </a> consist of RBS <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0034">(BBa_B0034)</a>, amilCP <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K592025">(BBa_K592025) </a> and double terminator <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_B0015"> (Bba_B0015) </a>, while the complete module was contained in <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K1387001">BBa_K1387001 </a>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team <a style="<del class="diffchange diffchange-inline">blue</del>" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team <a style="<ins class="diffchange diffchange-inline">color:#342D7E</ins>" href="http://parts.igem.org/Part:BBa_K936024">BBa_K936024</a> by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. <ins class="diffchange diffchange-inline"><i> </ins>Protein Engineering, 9, 239-247<ins class="diffchange diffchange-inline"></i></ins>.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
</table>Erawijantarihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=300953&oldid=prevErawijantari at 03:22, 17 October 20142014-10-17T03:22:22Z<p></p>
<table style="background-color: white; color:black;">
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<col class='diff-content' />
<col class='diff-marker' />
<col class='diff-content' />
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<td colspan='2' style="background-color: white; color:black;">← Older revision</td>
<td colspan='2' style="background-color: white; color:black;">Revision as of 03:22, 17 October 2014</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (<del class="diffchange diffchange-inline">B0034</del>), amilCP (BBa_K592025), and double terminator (<del class="diffchange diffchange-inline">B0015</del>). BBa_K1387000 consist of RBS (<del class="diffchange diffchange-inline">B0034</del>), amilCP (BBa_K592025) and double terminator (<del class="diffchange diffchange-inline">B0015</del>), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K339010"></ins>(BBa_K339010)<ins class="diffchange diffchange-inline"></a></ins>, RBS <ins class="diffchange diffchange-inline"> <a style="blue" href="http://parts.igem.org/Part:BBa_B0034"></ins>(<ins class="diffchange diffchange-inline">BBa_B0034</ins>)<ins class="diffchange diffchange-inline"></a></ins>, amilCP <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K592025"></ins>(BBa_K592025) <ins class="diffchange diffchange-inline"></a></ins>, and double terminator <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0015"> </ins>(<ins class="diffchange diffchange-inline">Bba_B0015</ins>) <ins class="diffchange diffchange-inline"></a></ins>. BBa_K1387000 consist of RBS (<ins class="diffchange diffchange-inline">Bba_B0034</ins>), amilCP (BBa_K592025) and double terminator <ins class="diffchange diffchange-inline"> </ins>(<ins class="diffchange diffchange-inline">BBa_B0015</ins>), while the complete module was contained in <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:</ins>BBa_K1387001<ins class="diffchange diffchange-inline">">(Bba_K!387001)</a></ins>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Degradation Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The casette of degradation module (BBa_K1387006) is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The casette of degradation module <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K1387006"></ins>(BBa_K1387006) <ins class="diffchange diffchange-inline"></a> </ins>is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Self-Regulatory Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS (<del class="diffchange diffchange-inline">B0034</del>), make a new part called </p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0034"></ins>(<ins class="diffchange diffchange-inline">BBa_B0034</ins>)<ins class="diffchange diffchange-inline"></a></ins>, make a new part called </p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>This casette (BBa_K1387002) consist of TetR (BBa_C0040) and Double Terminator <del class="diffchange diffchange-inline">(</del>BBa_B0015). TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>This casette <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0034"></ins>(BBa_K1387002)<ins class="diffchange diffchange-inline"></a> </ins>consist of TetR <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_C0040"></ins>(BBa_C0040)<ins class="diffchange diffchange-inline"></a> </ins>and Double Terminator <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:</ins>BBa_B0015<ins class="diffchange diffchange-inline">"> (Bba_B0015</ins>) <ins class="diffchange diffchange-inline"></a></ins>. TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (<del class="diffchange diffchange-inline">B0034</del>), amilCP (BBa_K592025), and double terminator (<del class="diffchange diffchange-inline">B0015</del>). BBa_K1387000 consist of RBS (<del class="diffchange diffchange-inline">B0034</del>), amilCP (BBa_K592025) and double terminator (<del class="diffchange diffchange-inline">B0015</del>), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K339010"></ins>(BBa_K339010)<ins class="diffchange diffchange-inline"></a>(</ins>, RBS <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0034"></ins>(<ins class="diffchange diffchange-inline">BBa_B0034</ins>)<ins class="diffchange diffchange-inline"></a></ins>, amilCP <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K592025"></ins>(BBa_K592025) <ins class="diffchange diffchange-inline"></a></ins>, and double terminator <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0015"> </ins>(<ins class="diffchange diffchange-inline">Bba_B0015</ins>) <ins class="diffchange diffchange-inline"></a></ins>. <ins class="diffchange diffchange-inline"><a style="blue" href="hhttp://parts.igem.org/Part:BBa_K1387000"> </ins>BBa_K1387000 <ins class="diffchange diffchange-inline"></a> </ins>consist of RBS <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0034"></ins>(<ins class="diffchange diffchange-inline">BBa_B0034</ins>)<ins class="diffchange diffchange-inline"></a></ins>, amilCP <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K592025"></ins>(BBa_K592025) <ins class="diffchange diffchange-inline"></a> </ins>and double terminator <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_B0015"> </ins>(<ins class="diffchange diffchange-inline">Bba_B0015</ins>) <ins class="diffchange diffchange-inline"></a></ins>, while the complete module was contained in <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:BBa_K1387001"></ins>BBa_K1387001 <ins class="diffchange diffchange-inline"></a></ins>. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>Convertion Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team <ins class="diffchange diffchange-inline"><a style="blue" href="http://parts.igem.org/Part:</ins>BBa_K936024<ins class="diffchange diffchange-inline">">BBa_K936024</a> </ins>by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td></tr>
</table>Erawijantarihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=271554&oldid=prevMardikusumo at 12:19, 16 October 20142014-10-16T12:19:56Z<p></p>
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</table>Mardikusumohttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=264746&oldid=prevMardikusumo at 06:04, 16 October 20142014-10-16T06:04:30Z<p></p>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/RepMod">REPORTER MODULE</a></li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/RepMod">REPORTER MODULE</a></li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/SelfMod">SELF REGULATORY MODULE</a></li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/SelfMod">SELF REGULATORY MODULE</a></li></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;"> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/FutureSystem">FUTURE SYSTEM</a></li></ins></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ul></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ul></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li>MODELING</li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li<ins class="diffchange diffchange-inline">><a href="https://2014.igem.org/Team:ITB_Indonesia/Modeling"</ins>>MODELING<ins class="diffchange diffchange-inline"></a></ins></li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>WETLAB</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>WETLAB</div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <ul></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <ul></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">PARTS</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/protocol">PROTOCOL</a></li></ins></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">ATTRIBUTIONS</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins class="diffchange diffchange-inline"> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/Parts</ins>">PARTS</a></li></div></td></tr>
<tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/Attributions</ins>">ATTRIBUTIONS</a></li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/Safety">SAFETY</a></li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/Safety">SAFETY</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">DATA</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/Data</ins>">DATA</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">PROTEIN MODEL</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/ProteinModel</ins>">PROTEIN MODEL</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">ACHIEVEMENT</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/Achievement</ins>">ACHIEVEMENT</a></li></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>NOTEBOOK</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>NOTEBOOK</div></td></tr>
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<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><del class="diffchange diffchange-inline"> <li><a href="">MODELING</a></li></del></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="https://<ins class="diffchange diffchange-inline">2014.</ins>igem.org/Team<ins class="diffchange diffchange-inline">:ITB_Indonesia/nb-wetlab</ins>">WETLAB</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="https://igem.org/Team<del class="diffchange diffchange-inline">.cgi?id=1387</del>">WETLAB</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/OnMedia">MEDIA</a></li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/OnMedia">MEDIA</a></li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/Biosafety">BIOSAFETY SEMINAR</a></li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li><a href="https://2014.igem.org/Team:ITB_Indonesia/Biosafety">BIOSAFETY SEMINAR</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">INDONESIA TEAMS MEET UP</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/MeetUp</ins>">INDONESIA TEAMS MEET UP</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">FUN WITH KIDS</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/Kids</ins>">FUN WITH KIDS</a></li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li><a href="">SHARING SYNBIO IN UPI</a></li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <li><a href="<ins class="diffchange diffchange-inline">https://2014.igem.org/Team:ITB_Indonesia/UPI</ins>">SHARING SYNBIO IN UPI</a></li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ul></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ul></div></td></tr>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p><del class="diffchange diffchange-inline">Georgiou</del>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p><ins class="diffchange diffchange-inline">1Georgiou</ins>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
</table>Mardikusumohttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=241091&oldid=prevNimas.ghasani at 09:02, 15 October 20142014-10-15T09:02:14Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 09:02, 15 October 2014</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <br><li>References</li></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p><del class="diffchange diffchange-inline">1Georgiou</del>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p><ins class="diffchange diffchange-inline">Georgiou</ins>,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr>
</table>Nimas.ghasanihttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=234355&oldid=prevMardikusumo at 21:28, 14 October 20142014-10-14T21:28:33Z<p></p>
<table style="background-color: white; color:black;">
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The casette of degradation module (BBa_K1387006) is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The casette of degradation module (BBa_K1387006) is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li>Self-Regulatory Module</li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <ins class="diffchange diffchange-inline"><br></ins><li>Self-Regulatory Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS (B0034), make a new part called </p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>pIBPAB is a hybrid promoter that induced by inclusion body from unfunctional protein. This promoter followed by strong RBS (B0034), make a new part called </p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/d/de/Sr2.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>This casette (BBa_K1387002) consist of TetR (BBa_C0040) and Double Terminator (BBa_B0015). TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>This casette (BBa_K1387002) consist of TetR (BBa_C0040) and Double Terminator (BBa_B0015). TetR is tetracycline repressor that bind to operator region and repressing the expression of downstream gene. In our system, the degradation module consist of TetO (Tet Operator) which is region of TetR (Tet Repressor) placed.</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <ins class="diffchange diffchange-inline"><br></ins><img src="https://static.igem.org/mediawiki/2014/f/f2/Sr3.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (B0034), amilCP (BBa_K592025), and double terminator (B0015). BBa_K1387000 consist of RBS (B0034), amilCP (BBa_K592025) and double terminator (B0015), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (B0034), amilCP (BBa_K592025), and double terminator (B0015). BBa_K1387000 consist of RBS (B0034), amilCP (BBa_K592025) and double terminator (B0015), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li>Convertion Module</li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <ins class="diffchange diffchange-inline"><br></ins><li>Convertion Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/7/7a/ConMod.JPG"></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>Improvisation the part submitted by UC Davis team BBa_K936024 by combining the construct with terminator, so we can characterize the expression of the enzymes and performe the assay for ethylene glycol utilization better than before. We name this BioBrick as convertion module.</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li>References</li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <ins class="diffchange diffchange-inline"><br></ins><li>References</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <p>1Georgiou,G., Stephens,L., Stathopoulos,C., Poetschke,L., Mendenhall,J., and Earhart,F. 1996. Display of β-Lactamase on Eschericia coli Surface : Outer Membrane Phenotypes Conferred by Lpp’-ompA’- β-Lactamase Fusions. Protein Engineering, 9, 239-247.</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> </ol></div></td></tr>
</table>Mardikusumohttp://2014.igem.org/wiki/index.php?title=Team:ITB_Indonesia/Parts&diff=234339&oldid=prevMardikusumo at 21:27, 14 October 20142014-10-14T21:27:18Z<p></p>
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<td colspan='2' style="background-color: white; color:black;">Revision as of 21:27, 14 October 2014</td>
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<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Reporter Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/8/8c/RepMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (B0034), amilCP (BBa_K592025), and double terminator (B0015). BBa_K1387000 consist of RBS (B0034), amilCP (BBa_K592025) and double terminator (B0015), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.<del class="diffchange diffchange-inline"><br></del></p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The construction of reporter module is consist of inducible promoter PibpAB (BBa_K339010), RBS (B0034), amilCP (BBa_K592025), and double terminator (B0015). BBa_K1387000 consist of RBS (B0034), amilCP (BBa_K592025) and double terminator (B0015), while the complete module was contained in BBa_K1387001. The reporter module will have a blue chromoprotein when the inclusion body is formed in the cell. This mechanism then acts as an indicator of cytoplasmic stress, in this situation is caused by inclussion body.</p></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <li>Degradation Module</li></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <ins class="diffchange diffchange-inline"><br></ins><li>Degradation Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/6/69/DegMod.JPG"></div></td></tr>
<tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div> <p>The casette of degradation module (BBa_K1387006) is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).<del class="diffchange diffchange-inline"><br></del></p></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div> <p>The casette of degradation module (BBa_K1387006) is comprised of constitutive promoter, tet operator, RBS, outer membrane protein A (ompA) fused with LC Cutinase, and double terminator. By using constitutive promoter, we expect the recombinant protein, in this case ompA-LC Cutinase, will be synthesized indefinitely. OmpA is outer membrane protein, it comprises of β–strand B3-B7. Rather than using full sequence of ompA, we use ompA (46-159) fused with lipoprotein signal sequence, thus exposing it on the cell surface of bacteria1. We fuse lpp-ompA with LC Cutinase, an enzyme that exhibit esterase activity. LC-Cutinase esterase activity will cleave the ester bond on PET and releasing terephthalic acid and ethylene glycol as a product. Fusion strategy of lpp-ompA on LC Cutinase gene is one of our way to create a whole cell biocatalyst which will be an effective molecular machinery to degrade PET on the environment. Due to constitutive expression of the recombinant protein in E.coli, there is a possibility of formation of insoluble protein inside the cell (inclusion body), because of that, we put tet operator upstream of RBS for further regulation (Georgiou et al, 1996).</p></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Self-Regulatory Module</li></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <li>Self-Regulatory Module</li></div></td></tr>
<tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div> <img src="https://static.igem.org/mediawiki/2014/b/b4/Sr1.JPG"></div></td></tr>
</table>Mardikusumo