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PMID: 1829527 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 88 ·No. 13 ·1991-07-01 ·Pages 5719-23

Palleros DR, Welch WJ, Fink AL

Abstract

Circular dichroism and HPLC gel filtration were used to show that cytosolic hsp70 is thermally stable but undergoes a conformational transition (midpoint, 43 degrees C; 57 degrees C in the presence of ATP or ADP) leading to oligomerization. hsp70 binds to unfolded, but not to folded, proteins in a temperature-dependent manner; complex formation is significant only at physiologically relevant temperatures. hsp70 binds ADP more tightly than ATP to form a binary complex, which binds to the unfolded protein more rapidly than free hsp70. ADP also inhibits the ATP-induced dissociation of the hsp70-protein complex. A regulatory role for the hsp70-nucleotide binary complexes is proposed.

MeSH Terms
Adenosine Diphosphate/metabolism Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Animals Cattle Circular Dichroism Heat-Shock Proteins/metabolism Hot Temperature Humans In Vitro Techniques Lactalbumin/metabolism Micrococcal Nuclease/metabolism Protein Binding Protein Conformation Protein Denaturation
Chemicals
Heat-Shock Proteins Adenosine Diphosphate Adenosine Triphosphate Lactalbumin Micrococcal Nuclease Adenosine Triphosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Palleros D R
Department of Chemistry and Biochemistry, University of California, Santa Cruz 95064.
Welch W J
Fink A L
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19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.88.13.5719
Published
1991-07-01
Pages
5719-23
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC51949
Subset
IM
Grants
NIGMS NIH HHS · GM33551 · United States
NIGMS NIH HHS · GM45316 · United States
External Links
PubMed source DOI: 10.1073/pnas.88.13.5719 PMC Full Text View journal details
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