The ribosomal exit tunnel as a target for optimizing protein expression in Escherichia coli.

ABSTRACT: The folding of many cellular proteins occurs co-translationally immediately outside the ribosome exit tunnel, where ribosomal proteins and other associated factors coordinate the synthesis and folding of newly translated polypeptides. Here, we show that the large subunit protein L29, which forms part of the exit tunnel in Escherichia coli, is required for the productive synthesis of an array of structurally diverse recombinant proteins including the green fluorescent protein (GFP) and an intracellular single-chain Fv antibody. Surprisingly, the corresponding mRNA transcript level of these proteins was markedly less abundant in cells lacking L29, suggesting an unexpected regulatory mechanism that links defects in the exit tunnel to the expression of genetic information. To further highlight

SUBMITTER: Contreras-Martinez LM 

PROVIDER: S-EPMC3382190 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature