Heat-shock response transcriptional program enables high-yield and high-quality recombinant protein production in Escherichia coli.

ABSTRACT: The biosynthesis of soluble, properly folded recombinant proteins in large quantities from Escherichia coli is desirable for academic research and industrial protein production. The basal E. coli protein homeostasis (proteostasis) network capacity is often insufficient to efficiently fold overexpressed proteins. Herein we demonstrate that a transcriptionally reprogrammed E. coli proteostasis network is generally superior for producing soluble, folded, and functional recombinant proteins. Reprogramming is accomplished by overexpressing a negative feedback deficient heat-shock response transcription factor before and during overexpression of the protein-of-interest. The advantage of transcriptional reprogramming versus simply overexpressing select proteostasis network components (e.g., chape

SUBMITTER: Zhang X 

PROVIDER: S-EPMC4168666 | biostudies-literature | 2014 Sep

REPOSITORIES: biostudies-literature