Involvement of the Shewanella oneidensis decaheme cytochrome MtrA in the periplasmic stability of the beta-barrel protein MtrB

Appl Environ Microbiol. 2011 Feb;77(4):1520-3. doi: 10.1128/AEM.01201-10. Epub 2010 Dec 17.

Abstract

The Shewanella oneidensis outer membrane β-barrel protein MtrB is part of a membrane-spanning protein complex (MtrABC) which is necessary for dissimilatory iron reduction. Quantitative PCR, heterologous gene expression, and mutant studies indicated that MtrA is required for periplasmic stability of MtrB. DegP depletion compensated for this MtrA dependence.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / genetics*
  • ATP-Binding Cassette Transporters / metabolism*
  • Bacterial Outer Membrane Proteins / genetics*
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism*
  • Blotting, Western
  • Electron Transport
  • Escherichia coli / genetics
  • Gene Expression
  • Gene Knockout Techniques
  • Heat-Shock Proteins / genetics
  • Heat-Shock Proteins / metabolism
  • Iron / metabolism
  • Mutation
  • Oxidation-Reduction
  • Periplasm / genetics
  • Periplasm / metabolism*
  • Periplasmic Proteins / genetics
  • Periplasmic Proteins / metabolism
  • Polymerase Chain Reaction
  • Protein Stability
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism
  • Shewanella / genetics*
  • Shewanella / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Heat-Shock Proteins
  • MtrA protein, Bacteria
  • MtrB protein, Shewanella putrefaciens
  • Periplasmic Proteins
  • Iron
  • DegP protease
  • Serine Endopeptidases