DSB proteins and bacterial pathogenicity

Nat Rev Microbiol. 2009 Mar;7(3):215-25. doi: 10.1038/nrmicro2087. Epub 2009 Feb 9.

Abstract

If DNA is the information of life, then proteins are the machines of life--but they must be assembled and correctly folded to function. A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding. Many bacteria use an oxidative protein-folding machinery to assemble proteins that are essential for cell integrity and to produce virulence factors. Although our current knowledge of this machinery stems largely from Escherichia coli K-12, this view must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.

Publication types

  • Review

MeSH terms

  • Bacteria / enzymology
  • Bacteria / pathogenicity*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology*
  • Computational Biology
  • Disulfides / metabolism*
  • Escherichia coli K12 / enzymology
  • Escherichia coli K12 / pathogenicity*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology*
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology*
  • Oxidation-Reduction
  • Phylogeny
  • Protein Disulfide-Isomerases / chemistry
  • Protein Disulfide-Isomerases / physiology*
  • Protein Folding
  • Protein Stability
  • Virulence

Substances

  • Bacterial Proteins
  • Disulfides
  • DsbB protein, Bacteria
  • Escherichia coli Proteins
  • Membrane Proteins
  • Protein Disulfide-Isomerases
  • dsbA protein, E coli