HtrA protease and processing of extracellular proteins of Streptococcus mutans

FEMS Microbiol Lett. 2001 Oct 16;204(1):23-8. doi: 10.1111/j.1574-6968.2001.tb10856.x.

Abstract

A homologue of the HtrA family of stress-response proteases was detected by analysis of the Streptococcus mutans genome sequence. Disabling of the S. mutans htrA gene by insertional inactivation resulted in bacterial clumping in liquid medium, altered colony morphology and a reduced ability to withstand high temperature, extremes of pH or oxidative stress. Seven different extracellular or wall-associated proteins that are known to be subject to post-translational proteolysis were examined in cultures of wild-type S. mutans and an htrA mutant. Inactivation of the htrA protease had no effect on degradation of the proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Cloning, Molecular
  • Culture Media
  • Gene Deletion
  • Heat-Shock Proteins*
  • Heat-Shock Response*
  • Humans
  • Molecular Sequence Data
  • Periplasmic Proteins*
  • Rabbits
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism*
  • Streptococcus mutans / enzymology*
  • Streptococcus mutans / genetics
  • Streptococcus mutans / physiology*

Substances

  • Bacterial Proteins
  • Culture Media
  • Heat-Shock Proteins
  • Periplasmic Proteins
  • DegP protease
  • Serine Endopeptidases