The activity and specificity of the outer membrane protein chaperone SurA are modulated by a proline isomerase domain.

ABSTRACT:

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SurA is a component of the periplasmic chaperone network that plays a central role in biogenesis of integral outer membrane β-barrel proteins (OMPs) in Escherichia coli. Although SurA contains two well-conserved proline isomerase (PPIase) domains, the contribution of these domains to SurA function is unclear. In the present work, we show that defects in OMP assembly caused by mutation of the β-barrel assembly factors BamA or BamB can be corrected by gain-of-function mutations in SurA that map to the first PPIase domain. These mutations apparently bypass the requirement for a stable interaction between SurA and the Bam complex and enhance SurA chaperone activity in vivo despite destabilization of the protein in vitro. Our findings suggest an autoinhibitory mechanism for r

SUBMITTER: Ricci DP 

PROVIDER: S-EPMC3747590 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature