Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase.
J Biosci
;
1996 Apr; 21(2): 179-190
Artigo
em Inglês
| IMSEAR
| ID: sea-161019
ABSTRACT
The 90 kDa heat shock protein (HSP90) is an ATP-binding molecular chaperone with an associated ATPase activity having nucleoplasmin and HSP70-binding homology domains and containing Ca-binding EF-hands and a nuclear localization signal. Here we characterize the HSP90-associated ATPase and show that it is (i) a P-type ATPase inhibited by molybdate and vanadate, (ii) able to hydrolyze methylfluorescein phosphate with a 5–6-fold higher affinity, (iii) a 3-times better GTPase than ATPase in the presence of calcium and (iv) HSP27 and F-actin, but not HSP10 can “convert” the HSP90-associated ATPase activity to HSP90 autokinase activity. The HSP90-associated ATP/GTPase may participate in the regulation of complex formation of HSP90 with other proteins, such as F-actin, tubulin and heat shock proteins.
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DisponíveL
Índice:
IMSEAR (Sudeste Asiático)
Idioma:
Inglês
Revista:
J Biosci
Ano de publicação:
1996
Tipo de documento:
Artigo
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