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PMID:10319814

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Citation

Spiess, C, Beil, A and Ehrmann, M (1999) A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97:339-47

Abstract

Misfolding or unfolding of polypeptides can occur as a consequence of environmental stress and spontaneous mutation. The abundance of general chaperones and proteases suggests that cells distinguish between proteins that can be refolded and "hopeless" cases fated to enter the proteolytic pathway. The mechanisms controlling this key metabolic decision are not well understood. We show here that the widely conserved heat shock protein DegP (HtrA) has both general molecular chaperone and proteolytic activities. The chaperone function dominates at low temperatures, while the proteolytic activity is present at elevated temperatures. These results show that a single cellular factor can switch between two key pathways, controlling protein stability and turnover. Implications of this finding for intracellular protein metabolism are discussed.

Links

PubMed

Keywords

Amylases/chemistry; Amylases/metabolism; Bacterial Proteins/chemistry; Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Chaperonins/metabolism; DNA Primers; Endopeptidases/metabolism; Escherichia coli/chemistry; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins; Gene Deletion; Gene Expression Regulation, Bacterial; Gene Expression Regulation, Enzymologic; Heat-Shock Proteins; Lac Operon; Mutation/physiology; Periplasmic Proteins; Protein Disulfide-Isomerases/genetics; Protein Folding; Serine Endopeptidases/chemistry; Serine Endopeptidases/genetics; Serine Endopeptidases/metabolism; Substrate Specificity; Temperature; Transcription, Genetic/physiology; alpha-Amylases/metabolism

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

ECOLI:DEGP

involved_in

GO:0006515: protein quality control for misfolded or incompletely synthesized proteins

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DEGP

involved_in

GO:0061077: chaperone-mediated protein folding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DEGP

involved_in

GO:0006457: protein folding

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DEGP

involved_in

GO:0006515: protein quality control for misfolded or incompletely synthesized proteins

ECO:0000315: mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DEGP

involved_in

GO:0009266: response to temperature stimulus

ECO:0000270: expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

See also

References

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