Comparative genomics and functional roles of the ATP-dependent proteases Lon and Clp during cytosolic protein degradation

Res Microbiol. 2004 Nov;155(9):710-9. doi: 10.1016/j.resmic.2004.06.003.

Abstract

The general pathway involving adenosine triphosphate (ATP)-dependent proteases and ATP-independent peptidases during cytosolic protein degradation is conserved, with differences in the enzymes utilized, in organisms from different kingdoms. Lon and caseinolytic protease (Clp) are key enzymes responsible for the ATP-dependent degradation of cytosolic proteins in Escherichia coli. Orthologs of E. coli Lon and Clp were searched for, followed by multiple sequence alignment of active site residues, in genomes from seventeen organisms, including representatives from eubacteria, archaea, and eukaryotes. Lon orthologs, unlike ClpP and ClpQ, are present in most organisms studied. The roles of these proteases as essential enzymes and in the virulence of some organisms are discussed.

Publication types

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

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Cytosol / metabolism*
  • Endopeptidase Clp / genetics
  • Endopeptidase Clp / metabolism*
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Genomics*
  • Molecular Sequence Data
  • Protease La / genetics
  • Protease La / metabolism*
  • Proteins / metabolism*

Substances

  • Escherichia coli Proteins
  • Proteins
  • Adenosine Triphosphate
  • Lon protein, E coli
  • Protease La
  • Endopeptidase Clp