Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase

Nardai, Gabor, Schnaider, Tamas, Soti, Csaba, Ryan, Michael T., Høj, Peter B., Somogyi, Janos and Csermely, Peter (1996) Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase. Journal of Biosciences, 21 2: 179-190. doi:10.1007/BF02703107


Author Nardai, Gabor
Schnaider, Tamas
Soti, Csaba
Ryan, Michael T.
Høj, Peter B.
Somogyi, Janos
Csermely, Peter
Title Characterization of the 90 kDa heat shock protein (HSP90)-associated ATP/GTPase
Journal name Journal of Biosciences   Check publisher's open access policy
ISSN 0250-5991
0973-7138
Publication date 1996-04-01
Sub-type Article (original research)
DOI 10.1007/BF02703107
Open Access Status DOI
Volume 21
Issue 2
Start page 179
End page 190
Total pages 12
Place of publication Bangalore, Karnataka, India
Publisher Indian Academy of Sciences
Language eng
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.
Keyword Molecular chaperone
Vanadate
Molybdate
Methylfluorescein phosphate
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Office of the Vice-Chancellor
 
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