Team:UST Beijing/Parts

Parts We Used

Mitochondrial proteorhodopsin (humanized genetic code bias)

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PR, an abbreviation for proteorhodopsin, is a transmembrane protein which was discovered in 2000 through shortgun genome sequencing of unculturable bacteria isolated from the seawater off the coast of California. PR is a light-activated proton pump and generates a pmf which is short for proton motive force. This part was constructed as below: We replaced the PR's precusor sequence with the leader peptide of human cytochrome oxidase subunit 4 isoform 1, targeting it to mitochondrial inner membrane. Meanwhile, all the codons were re-designed according to codon usage bias for Homo sapiens.

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The proton concentration gradient, produced by the electron transport chain using NADH, directly contribute to the synthesis of ATP. The producing of NADH mainly rely on glycolysis and tri-carboxylic acid circle for animals. However, existence of mPR in the inner membrane could be the possible way to decrease the dependence of NADH and respiratory chain.

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mPR as a light driven trans-membrane protein, when the exposed to light, can transport protons from mitochondrial matrix to inter-membrane space and then the proton gradients.

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