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Team:Groningen/Template/MODULE/Project/secretion/part3
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| - | Aiia is probably | + | Aiia is probably an intracellular enzyme, which makes secreting it kind of hard. Also, it is not quite sure that Dispersin B is secreted and if so, it would have a signal peptide for secreting from its host. These are some problems which can sincerely hurt our secretion system. |
| - | The solution is signal peptide from the gene USP45 which is secreted out of <i>Lactococcus lactis</i> very efficiently. This became clear when scientist fused a couple of genes together with the signal coding sequence of USP45. This resulted in an efficient way of secreting the coded proteins into the media.<sup>4</sup> | + | The solution is a signal peptide from the gene USP45 which is secreted out of <i>Lactococcus lactis</i> very efficiently. This became clear when scientist fused a couple of genes together with the signal coding sequence of USP45. This resulted in an efficient way of secreting the coded proteins into the media.<sup>4</sup> |
So how are these enzymes secreted out of the cell when the spUSP45 is fused to the enzymes? | So how are these enzymes secreted out of the cell when the spUSP45 is fused to the enzymes? | ||
Well, at first this coding sequence of ssUSP45 should be fused together with the genes. Then after translation, the coded enzyme will meet a chaperone protein , called SecB, which bring the secreting enzyme to a protein conducting gate. This gate cleaves the signal peptide and frees the enzyme from the cell. <sup>5</sup> | Well, at first this coding sequence of ssUSP45 should be fused together with the genes. Then after translation, the coded enzyme will meet a chaperone protein , called SecB, which bring the secreting enzyme to a protein conducting gate. This gate cleaves the signal peptide and frees the enzyme from the cell. <sup>5</sup> | ||
Revision as of 02:46, 18 October 2014
Signal peptide of USP45
Aiia is probably an intracellular enzyme, which makes secreting it kind of hard. Also, it is not quite sure that Dispersin B is secreted and if so, it would have a signal peptide for secreting from its host. These are some problems which can sincerely hurt our secretion system.
The solution is a signal peptide from the gene USP45 which is secreted out of Lactococcus lactis very efficiently. This became clear when scientist fused a couple of genes together with the signal coding sequence of USP45. This resulted in an efficient way of secreting the coded proteins into the media.4
So how are these enzymes secreted out of the cell when the spUSP45 is fused to the enzymes?
Well, at first this coding sequence of ssUSP45 should be fused together with the genes. Then after translation, the coded enzyme will meet a chaperone protein , called SecB, which bring the secreting enzyme to a protein conducting gate. This gate cleaves the signal peptide and frees the enzyme from the cell. 5
Therefore, we have chosen to fuse all our coding sequences from the enzymes with ssUSP45.
