Thiol-Disulfide Exchange in Gram-Positive Firmicutes

Trends Microbiol. 2016 Nov;24(11):902-915. doi: 10.1016/j.tim.2016.06.010. Epub 2016 Jul 15.

Abstract

Extracytoplasmic thiol-disulfide oxidoreductases (TDORs) catalyze the oxidation, reduction, and isomerization of protein disulfide bonds. Although these processes have been characterized in Gram-negative bacteria, the majority of Gram-positive TDORs have only recently been discovered. Results from recent studies have revealed distinct trends in the types of TDOR used by different groups of Gram-positive bacteria, and in their biological functions. Actinobacteria TDORs can be essential for viability, while Firmicute TDORs influence various physiological processes, including protein stability, oxidative stress resistance, bacteriocin production, and virulence. In this review we discuss the diverse extracytoplasmic TDORs used by Gram-positive bacteria, with a focus on Gram-positive Firmicutes.

Keywords: Gram-positive; disulfide bond; thiol-disulfide oxidoreductase.

Publication types

  • Review

MeSH terms

  • Actinobacteria / enzymology
  • Bacillus / enzymology
  • Bacillus / metabolism
  • Bacterial Proteins / metabolism
  • Clostridium / enzymology
  • Clostridium / metabolism
  • Firmicutes / enzymology*
  • Firmicutes / metabolism*
  • Lactococcus / enzymology
  • Lactococcus / metabolism
  • Membrane Proteins / metabolism
  • Oxidation-Reduction
  • Oxidative Stress
  • Protein Disulfide Reductase (Glutathione) / metabolism*
  • Protein Disulfide Reductase (Glutathione) / physiology*
  • Protein Stability
  • Staphylococcus aureus / enzymology
  • Staphylococcus aureus / metabolism

Substances

  • Bacterial Proteins
  • Membrane Proteins
  • Protein Disulfide Reductase (Glutathione)