[Heterologous expression and function evaluation of Gloeobacter violaceus rhodopsin in Escherichia coli].

Sheng Wu Gong Cheng Xue Bao

Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.

Published: February 2021

Proton-pumping rhodopsin (PPR) is a simple photosystem widely distributed in nature. By binding to retinal, PPR can transfer protons from the cytoplasmic to the extracellular side of the membrane under illumination, creating a proton motive force (PMF) to synthesize ATP. The conversion of light into chemical energy by introducing rhodopsin into nonphotosynthetic engineered strains could contribute to promoting growth, increasing production and improving cell tolerance of microbial hosts. Gloeorhodopsin (GR) is a PPR from Gloeobacter violaceus PCC 7421. We expressed GR heterologously in Escherichia coli and verified its functional activity. GR could properly function as a light-driven proton pump and its absorption maximum was at 539 nm. We observed that GR was mainly located on the cell membrane and no inclusion body could be found. After increasing expression level by ribosome binding site optimization, intracellular ATP increased, suggesting that GR could supply additional energy to heterologous hosts under given conditions.

Download full-text PDF

Source
http://dx.doi.org/10.13345/j.cjb.200307DOI Listing

Publication Analysis

Top Keywords

gloeobacter violaceus
8
[heterologous expression
4
expression function
4
function evaluation
4
evaluation gloeobacter
4
violaceus rhodopsin
4
rhodopsin escherichia
4
escherichia coli]
4
coli] proton-pumping
4
proton-pumping rhodopsin
4

Similar Publications

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!