Functionality of membrane proteins overexpressed and purified from E. coli is highly dependent upon the strain.

ABSTRACT: Overexpression of correctly folded membrane proteins is a fundamental prerequisite for functional and structural studies. One of the most commonly used expression systems for the production of membrane proteins is Escherichia coli. While misfolded proteins typically aggregate and form inclusions bodies, membrane proteins that are addressed to the membrane and extractable by detergents are generally assumed to be properly folded. Accordingly, GFP fusion strategy is often used as a fluorescent proxy to monitor their expression and folding quality. Here we investigated the functionality of two different multidrug ABC transporters, the homodimer BmrA from Bacillus subtilis and the heterodimer PatA/PatB from Streptococcus pneumoniae, when produced in several E. coli strains with T7 expression s

SUBMITTER: Mathieu K 

PROVIDER: S-EPMC6390180 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature