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PMID:7900997

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Citation

Schröder, H, Langer, T, Hartl, FU and Bukau, B (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12:4137-44

Abstract

Members of the conserved Hsp70 chaperone family are assumed to constitute a main cellular system for the prevention and the amelioration of stress-induced protein damage, though little direct evidence exists for this function. We investigated the roles of the DnaK (Hsp70), DnaJ and GrpE chaperones of Escherichia coli in prevention and repair of thermally induced protein damage using firefly luciferase as a test substrate. In vivo, luciferase was rapidly inactivated at 42 degrees C, but was efficiently reactivated to 50% of its initial activity during subsequent incubation at 30 degrees C. DnaK, DnaJ and GrpE did not prevent luciferase inactivation, but were essential for its reactivation. In vitro, reactivation of heat-inactivated luciferase to 80% of its initial activity required the combined activity of DnaK, DnaJ and GrpE as well as ATP, but not GroEL and GroES. DnaJ associated with denatured luciferase, targeted DnaK to the substrate and co-operated with DnaK to prevent luciferase aggregation at 42 degrees C, an activity that was required for subsequent reactivation. The protein repair function of DnaK, GrpE and, in particular, DnaJ is likely to be part of the role of these proteins in regulation of the heat shock response.

Links

PubMed PMC413706

Keywords

Bacterial Proteins/genetics; Bacterial Proteins/metabolism; Chaperonins; Enzyme Activation; Enzyme Reactivators/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Genes, Bacterial; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins; Heat-Shock Proteins/genetics; Heat-Shock Proteins/metabolism; Hot Temperature; Luciferases/metabolism; Multigene Family; Protein Denaturation; Proteins/genetics; Proteins/metabolism; Recombinant Proteins/metabolism

Significance

Annotations

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

ECOLI:DNAJ

acts_upstream_of_or_within

GO:0051085: chaperone cofactor-dependent protein refolding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

acts_upstream_of_or_within

GO:0051085: chaperone cofactor-dependent protein refolding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

acts_upstream_of_or_within

GO:0009408: response to heat

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

acts_upstream_of_or_within

GO:0034620: cellular response to unfolded protein

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

involved_in

GO:0009408: response to heat

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

involved_in

GO:0034620: cellular response to unfolded protein

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

ECOLI:DNAK

involved_in

GO:0051085: chaperone cofactor-dependent protein refolding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

BIFAP:K4INZ2

GO:0006457: protein folding

ECO:0000314:

P

See Figure 1(A) of associated PMID

complete
CACAO 9576

ECOLI:DNAJ

involved_in

GO:0051085: chaperone cofactor-dependent protein refolding

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

See also

References

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