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Reaction mechanism of the 70 kDa heat shock cognate Hsc70
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Background: The 70 kDa heat shock protein family is essential for cell survival. However, little is known about their reaction mechanism.
Question: Elucidate the partial reactions of Hsc70 with ATP, nucleotide analogues and substrate proteins. Measure the influence of drugs on these partial reactions.
Results: Hsc70 and its congeners bind nucleotides very tightly (low
k
off
). Binding of ATP opens the protein binding site and allows the dissociation of bound and the association of fresh proteins. The energy required is supplied by ATP binding, ATP hydrolysis is not required but drives the reaction forward.
Cyclosporin A (CsA) activates Hsc70 ATPase-activity form a different, regulatory site. Clathrin coated vesicles (CCV) from brain, involved in membrane recycling, differ structurally and functionally from the endocytic CCV found in all organs. Hsc70 from various organs and organisms however has virtually
identical properties.
Title: Reaction mechanism of the 70 kDa heat shock cognate Hsc70
Description:
Background: The 70 kDa heat shock protein family is essential for cell survival.
However, little is known about their reaction mechanism.
Question: Elucidate the partial reactions of Hsc70 with ATP, nucleotide analogues and substrate proteins.
Measure the influence of drugs on these partial reactions.
Results: Hsc70 and its congeners bind nucleotides very tightly (low
k
off
).
Binding of ATP opens the protein binding site and allows the dissociation of bound and the association of fresh proteins.
The energy required is supplied by ATP binding, ATP hydrolysis is not required but drives the reaction forward.
Cyclosporin A (CsA) activates Hsc70 ATPase-activity form a different, regulatory site.
Clathrin coated vesicles (CCV) from brain, involved in membrane recycling, differ structurally and functionally from the endocytic CCV found in all organs.
Hsc70 from various organs and organisms however has virtually
identical properties.
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