ClpP: a distinctive family of cylindrical energy-dependent serine proteases

FEBS Lett. 2007 Jul 31;581(19):3749-57. doi: 10.1016/j.febslet.2007.04.076. Epub 2007 May 8.

Abstract

Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy-dependent serine proteases that are highly conserved throughout bacteria and eukaryota. They typically interact with ATP-dependent AAA+ chaperones that bind and unfold target substrates and then translocate them into ClpP for degradation. Structural and functional studies have provided a detailed view of the mechanism of function of this class of proteases.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Endopeptidase Clp / chemistry*
  • Endopeptidase Clp / metabolism
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Protein Conformation
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism

Substances

  • Bacterial Proteins
  • Molecular Chaperones
  • Plant Proteins
  • Adenosine Triphosphate
  • Serine Endopeptidases
  • Endopeptidase Clp