The HtrA family of proteases: implications for protein composition and cell fate

Tim Clausen, Christopher Southan, Michael Ehrmann

Research output: Contribution to journalArticlepeer-review

Abstract

Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.

Original languageEnglish
Pages (from-to)443-55
Number of pages13
JournalMolecular Cell
Volume10
Issue number3
Publication statusPublished - Sep 2002

Keywords

  • Amino Acid Sequence
  • Bacterial Proteins
  • Drug Design
  • Gene Expression Regulation, Bacterial
  • Heat-Shock Proteins
  • Humans
  • Models, Molecular
  • Molecular Chaperones
  • Molecular Sequence Data
  • Periplasmic Proteins
  • Phylogeny
  • Protein Folding
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Serine Endopeptidases
  • Temperature

Fingerprint

Dive into the research topics of 'The HtrA family of proteases: implications for protein composition and cell fate'. Together they form a unique fingerprint.

Cite this