HSP100/Clp proteins: a common mechanism explains diverse functions

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 pat...

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Bibliographic Details
Published in:Trends in biochemical sciences (Amsterdam. Regular ed.) 1996-08, Vol.21 (8), p.289-296
Main Authors: Schirmer, Eric C., Glover, John R., Singer, Mike A., Lindquist, Susan
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Adenosine Triphosphatases - physiology
Amino Acid Sequence
Animals
ATPases Associated with Diverse Cellular Activities
Bacillus subtilis
Bacteriophage mu - physiology
Endopeptidase Clp
Escherichia coli
Escherichia coli Proteins
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - classification
Heat-Shock Proteins - physiology
Humans
Mice
Models, Biological
Molecular Chaperones
Molecular Sequence Data
Pasteurella haemolytica
Protein Conformation
Protozoan Proteins - physiology
Pseudomonas aeruginosa
Saccharomyces cerevisiae Proteins
Serine Endopeptidases - physiology
Serpulina hyodysenteriae
Stress, Physiological
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Summary: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 higherorder protein structures and aggregates unifies the molecular functions of this diverse family.
ISSN:0968-0004
1362-4326
DOI:10.1016/S0968-0004(96)10038-4