Team:UST Beijing/Parts

Parts We Used

Mitochondrial proteorhodopsin (humanized genetic code bias)

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.

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.

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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