Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli

Res Microbiol. 2009 Nov;160(9):660-6. doi: 10.1016/j.resmic.2009.07.012. Epub 2009 Aug 18.

Abstract

Two members of the widely conserved HtrA family of serine proteases, DegP and DegS, are key players in extracytoplasmic protein quality control. The underlying mechanisms of their main functions in stress sensing, regulation and protection during the unfolded protein response are discussed.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial
  • Heat-Shock Proteins / chemistry*
  • Heat-Shock Proteins / metabolism*
  • Periplasmic Proteins / chemistry*
  • Periplasmic Proteins / metabolism*
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism*

Substances

  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • Periplasmic Proteins
  • degS protein, Escherichia coli
  • DegP protease
  • Serine Endopeptidases