Proteolysis in prokaryotes: protein quality control and regulatory principles

Mol Microbiol. 2003 Sep;49(6):1451-62. doi: 10.1046/j.1365-2958.2003.03693.x.
No abstract available

Publication types

  • Congress

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism
  • Archaea / enzymology*
  • Bacteria / enzymology*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / physiology
  • Bacterial Proteins / ultrastructure
  • Chloroplasts / enzymology
  • Endopeptidase Clp
  • Endopeptidases* / chemistry
  • Endopeptidases* / genetics
  • Endopeptidases* / metabolism
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / metabolism
  • Membrane Proteins / chemistry
  • Membrane Proteins / physiology
  • Membrane Proteins / ultrastructure
  • Mitochondria / enzymology
  • Models, Molecular
  • Periplasmic Proteins / chemistry
  • Periplasmic Proteins / metabolism
  • Protein Conformation
  • Protein Structure, Quaternary
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics
  • Serine Endopeptidases / metabolism

Substances

  • Bacterial Proteins
  • Heat-Shock Proteins
  • Membrane Proteins
  • Periplasmic Proteins
  • Endopeptidases
  • DegP protease
  • Serine Endopeptidases
  • Endopeptidase Clp
  • Adenosine Triphosphatases