Interaction of hsp70 with unfolded proteins: effects of temperature and nucleotides on the kinetics of binding.
basic_science · Level V
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- Record sourced from PubMed, PMID 1829527.
- Also identified by PMC identifier 51949.
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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.
Medical subject headings
- Heat-Shock Proteins
- Protein Binding
- Protein Denaturation