SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.

ABSTRACT: A major step in the biogenesis of newly synthesized precursor proteins in bacteria is their targeting to the Sec translocon at the inner membrane. In gram-negative bacteria, the chaperone SecB binds nonnative forms of precursors and specifically transfers them to the SecA motor component of the translocase, thus facilitating their export. The major human pathogen Mycobacterium tuberculosis is an unusual gram-positive bacterium with a well-defined outer membrane and outer membrane proteins. Assistance to precursor proteins by chaperones in this bacterium remains largely unexplored. Here we show that the product of the previously uncharacterized Rv1957 gene of M. tuberculosis can substitute for SecB functions in Escherichia coli and prevent preprotein aggregation in vitro. Interestingly, in

SUBMITTER: Bordes P 

PROVIDER: S-EPMC3100995 | biostudies-literature | 2011 May

REPOSITORIES: biostudies-literature