The function of the DegP (HtrA) protein: Protease versus chaperone

IUBMB Life. 2016 Nov;68(11):904-907. doi: 10.1002/iub.1561. Epub 2016 Sep 26.

Abstract

The DegP (or HtrA) is a highly conserved family of proteins functioning in all living organisms. It was initially identified as a protease functioning in the periplasmic space of the Gram-negative bacterial cells. It was later reported to also exhibit chaperone activity and thus has been designated as a bifunctional protein. However, recent studies demonstrated that in living cells it more likely functions only as a protease with hardly detectable chaperone activities. In this review, I will summarize the evidences clarifying that DegP more likely only functions as a protease rather than as a chaperone in cells. © 2016 IUBMB Life, 68(11):904-907, 2016.

Keywords: outer membrane protein biogenesis; periplasmic space; protein quality control.

Publication types

  • Review

MeSH terms

  • Escherichia coli / enzymology
  • Heat-Shock Proteins / physiology*
  • Periplasmic Proteins / physiology*
  • Protein Processing, Post-Translational
  • Proteolysis
  • Serine Endopeptidases / physiology*

Substances

  • Heat-Shock Proteins
  • Periplasmic Proteins
  • DegP protease
  • Serine Endopeptidases