HtrA--a renaissance protein

Structure. 2002 Jun;10(6):737-9. doi: 10.1016/s0969-2126(02)00782-7.

Abstract

Initially identified as proteases, members of the HtrA/DegP family of proteins have also been shown to act as chaperones in bacteria, and more recently implicated, as regulators of apoptosis in mammals. Two new structures of mammalian HtrA2 and E. coli DegP provide insights into the origin of this plurality of function.

MeSH terms

  • Apoptosis / physiology*
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / physiology*
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / physiology*
  • Periplasmic Proteins / chemistry
  • Periplasmic Proteins / physiology*
  • Protein Conformation
  • Protein Structure, Tertiary
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / physiology*

Substances

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