PMID:16289019

Citation	Kedzierska, S, Chesnokova, LS, Witt, SN and Zolkiewski, M (2005) Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli. Arch. Biochem. Biophys. 444:61-5
Abstract	ClpB and DnaK form a bi-chaperone system that reactivates strongly aggregated proteins in vivo and in vitro. Previously observed interaction between purified ClpB and DnaK suggested that one of the chaperones might recruit its partner during substrate reactivation. We show that ClpB from Escherichia coli binds at the substrate binding site of DnaK and the interaction is supported by the N-terminal domain and the middle domain of ClpB. Moreover, the interaction between ClpB and DnaK depends on the nucleotide-state of DnaK: it is stimulated by ADP and inhibited by ATP. These observations indicate that DnaK recognizes selected structural motifs in ClpB as "pseudo-substrates" and that ClpB may compete with bona fide substrates of DnaK. We conclude that direct interaction between ClpB and DnaK does not mediate a substrate transfer between the chaperones, it may, however, play a role in the recruitment of the bi-chaperone system to specific recognition sites in aggregated particles.
Links	PubMed Online version:10.1016/j.abb.2005.10.005
Keywords	Adenosine Diphosphate/chemistry; Adenosine Triphosphate/chemistry; Chromatography, Gel; Escherichia coli/chemistry; Escherichia coli Proteins/chemistry; HSP70 Heat-Shock Proteins/chemistry; Heat-Shock Proteins/chemistry; Molecular Chaperones/chemistry; Protein Binding; Protein Structure, Tertiary
edit table

Significance

You can help EcoliWiki by summarizing why this paper is useful

Useful Materials and Methods

You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.

Annotations

<annotationlinks/>

EcoliWiki Links

Add links to pages that link here (e.g. gene, product, method pages)

References

See Help:References for how to manage references in EcoliWiki.