Functional characterization of recombinant human HSP70 domains and interdomain interactions

ATPase and peptide-binding activity of recombinant human heat shock proteins HSP70 A1B and HSC70 and two hybrid proteins derived from them was investigated. UV-spectral recorded data were used to characterize conformational rearrangements induced by domain replacement or HSP70-peptide interaction. I...

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Bibliographic Details
Published in:Molecular biology (New York) 2011-10, Vol.45 (5), p.833-842
Main Authors: Chernikov, V. A., Gorokhovets, N. V., Savvateeva, L. V., Severin, S. E.
Format: Article
Language:English
Subjects:
Adenosinetriphosphatase
Binding sites
Biochemistry
Biomedical and Life Sciences
Chaperones
Data processing
Genetic recombination
Heat shock proteins
Hsc70 protein
Hsp70 protein
Human Genetics
Hybrids
Life Sciences
Molecular biology
Peptides
Spectrum analysis
Structural and Functional Analysis of Biopolymers and Their Complexes
Substrate specificity
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Summary:ATPase and peptide-binding activity of recombinant human heat shock proteins HSP70 A1B and HSC70 and two hybrid proteins derived from them was investigated. UV-spectral recorded data were used to characterize conformational rearrangements induced by domain replacement or HSP70-peptide interaction. It was shown that the N-terminal domain dramatically affects the substrate specificity of the C-terminal peptide-binding domain, which puts forward a new hypothesis for HSP70 chaperone machinery. On the other hand, the peptide-binding domain affected the ATPase activity of the recombinant proteins. There was a linear relationship between the ATPase activity and the peptide complex percentage. This connection can be used for quantification of HSP70 complexes with unlabeled peptides.
ISSN:0026-8933
1608-3245
DOI:10.1134/S0026893311040029