A quantitative interpretation of oxidative protein folding activity in Escherichia coli.

ABSTRACT:

Background

Escherichia coli is of central interest to biotechnological research and a widely used organism for producing proteins at both lab and industrial scales. However, many proteins remain difficult to produce efficiently in E. coli. This is particularly true for proteins that require post translational modifications such as disulfide bonds.

Results

In this study we develop a novel approach for quantitatively investigating the ability of E. coli to produce disulfide bonds in its own proteome. We summarise the existing knowledge of the E. coli disulfide proteome and use this information to investigate the demand on this organism's quantitative oxidative folding apparatus under different growth conditions. Furthermore, we built an ordinary differential equation-based mod

SUBMITTER: Rettenbacher LA 

PROVIDER: S-EPMC9773447 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature