HSP100/Clp proteins: a common mechanism explains diverse functions

Trends Biochem Sci. 1996 Aug;21(8):289-96.

Abstract

The HSP100/Clp proteins are a newly discovered family with a great diversity of functions, such as increased tolerance to high temperatures, promotion of proteolysis of specific cellular substrates and regulation of transcription. HSP100/Clp proteins are also synthesized in a variety of specific patterns and, in eukaryotes, are localized to different subcellular compartments. Recent data suggest that a common ability to disassemble higher-order protein structures and aggregates unifies the molecular functions of this diverse family.

Publication types

  • Review

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphatases / physiology
  • Amino Acid Sequence
  • Animals
  • Bacteriophage mu / physiology
  • Endopeptidase Clp
  • Escherichia coli Proteins
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / classification*
  • Heat-Shock Proteins / physiology*
  • Humans
  • Mice
  • Models, Biological
  • Molecular Chaperones
  • Molecular Sequence Data
  • Protein Conformation
  • Protozoan Proteins / physiology
  • Saccharomyces cerevisiae Proteins*
  • Serine Endopeptidases / physiology
  • Stress, Physiological

Substances

  • Escherichia coli Proteins
  • Heat-Shock Proteins
  • Molecular Chaperones
  • Protozoan Proteins
  • Saccharomyces cerevisiae Proteins
  • HsP104 protein, S cerevisiae
  • Serine Endopeptidases
  • Endopeptidase Clp
  • Adenosine Triphosphatases
  • ClpB protein, Leishmania
  • ClpX protein, E coli
  • ATPases Associated with Diverse Cellular Activities

Associated data

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  • GENBANK/Z38058