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PMID:10521435

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Citation

Suh, WC, Lu, CZ and Gross, CA (1999) Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274:30534-9

Abstract

Hsp70 family members together with their Hsp40 cochaperones function as molecular chaperones, using an ATP-controlled cycle of polypeptide binding and release to mediate protein folding. Hsp40 plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70. We have explored the interaction between the Escherichia coli Hsp70 family member, DnaK, and its cochaperone partner DnaJ. Our data show that the binding of ATP, subsequent conformational changes in DnaK, and DnaJ-stimulated ATP hydrolysis are all required for the formation of a DnaK-DnaJ complex as monitored by Biacore analysis. In addition, our data imply that the interaction of the J-domain with DnaK depends on the substrate binding state of DnaK.

Links

PubMed

Keywords

Adenosine Triphosphatases/metabolism; Binding Sites; Biosensing Techniques; Escherichia coli/metabolism; Escherichia coli Proteins; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins/chemistry; Heat-Shock Proteins/metabolism; Kinetics; Models, Chemical; Models, Molecular; Molecular Chaperones/chemistry; Molecular Chaperones/metabolism; Protein Conformation; Protein Folding

Significance

Annotations

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

ECOLI:DNAJ

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P0A6Y8

F

Seeded From UniProt

complete

ECOLI:DNAK

enables

GO:0005515: protein binding

ECO:0000353: physical interaction evidence used in manual assertion

UniProtKB:P08622

F

Seeded From UniProt

complete

ECOLI:DNAK

GO:0005524: ATP binding

ECO:0000021:

F

DnaK and DnaJ bind under certain circumstances- the abstract mentions that they have been shown to be co-chaperones. Figure 1, graph 1 demonstrates binding assays using immobilized DnaK on a sensor chip. The binding of DnaK to DnaJ occurs only in the presence of ATP, and not any other form of nucleotide. While this is not a direct analysis of the ATP-binding domain, from the graph it is possible to infer that DnaK requires the presence of ATP to bind DnaJ, and that the ATP is binding to DnaK (since it was only present in solution during the process of immobilizing DnaK, not when the DnaJ was added).

Missing: with/from
CACAO 4658


See also

References

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