Osmoregulation of the HtrA (DegP) protease of Escherichia coli: an Hha-H-NS complex represses HtrA expression at low osmolarity

FEMS Microbiol Lett. 2005 Oct 1;251(1):75-80. doi: 10.1016/j.femsle.2005.07.027.

Abstract

The HtrA protein of Escherichia coli is a heat-shock inducible periplasmic protease, essential for bacterial survival at high temperatures. Expression of htrA gene depends on the alternative factor sigmaE and on the two-component regulatory system Cpx. These regulators systems respond, among others factors, to overproduction of misfolded proteins in the periplasm or to high level synthesis of various extracytoplasmic proteins. We describe in this report the osmoregulation of the expression of htrA gene. Low osmolarity conditions result in htrA repression. We report, as well, the role of the nucleoid associated proteins H-NS and Hha in the repression of htrA expression at low osmolarity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism
  • Bacterial Proteins / physiology*
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism*
  • DNA-Binding Proteins / physiology*
  • Electrophoretic Mobility Shift Assay
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Escherichia coli Proteins / genetics*
  • Escherichia coli Proteins / metabolism*
  • Gene Expression Regulation, Bacterial*
  • Gene Fusion
  • Genes, Reporter
  • Heat-Shock Proteins / biosynthesis*
  • Mutation
  • Osmolar Concentration
  • Periplasmic Proteins / biosynthesis*
  • RNA, Bacterial / analysis
  • RNA, Messenger / analysis
  • Serine Endopeptidases / biosynthesis*
  • beta-Galactosidase / analysis
  • beta-Galactosidase / genetics

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • H-NS protein, bacteria
  • Heat-Shock Proteins
  • Periplasmic Proteins
  • RNA, Bacterial
  • RNA, Messenger
  • hha protein, E coli
  • beta-Galactosidase
  • DegP protease
  • Serine Endopeptidases