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          Institute: MPI für medizinische Forschung     Collection: Abteilung Biomolekulare Mechanismen     Display Documents



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ID: 23030.0, MPI für medizinische Forschung / Abteilung Biomolekulare Mechanismen
Sti1 is a noncompetitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the ATPase cycle
Authors:Richter, Klaus; Muschler, Paul; Hainzl, Otmar; Reinstein, Jochen; Buchner, Johannes
Language:English
Date of Publication (YYYY-MM-DD):2003-03-21
Title of Journal:Journal of Biological Chemistry
Journal Abbrev.:J. Biol. Chem. (JBCHA3)
Volume:278
Issue / Number:12
Start Page:10328
End Page:10333
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:The molecular chaperone Hsp90 is known to be involved in the activation of key regulatory proteins such as kinases, steroid hormone receptors, and transcription factors in an ATP-dependent manner. During the chaperone cycle, Hsp90 has been found associated with the partner protein Hop/Sti1, which seems to be required for the progression of the cycle. However, little is known about its specific function. Here we have investigated the interaction of Sti1 from Saccharomyces cerevisiae with Hsp90 and its influence on the ATPase activity. We show that the inhibitory mechanism of Sti1 on the ATPase activity of Hsp90 is non-competitive. Sti1 binds to the N- and C-terminal part of Hsp90 and prevents the N-terminal dimerization reaction that is required for efficient ATP hydrolysis. The first 24 amino acids of Hsp90, a region shown previously to be important for the association of the N-terminal domains and stimulation of ATP hydrolysis, seems to be important for this interaction.
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
External Affiliations:Institut für Organische Chemie und Biochemie, Technische Universität München, Lichtenbergstr.4, 85747 Garching, Germany; Max Planck Institut für molekulare Physiologie, Otto Hahn Str. 11, 44227 Dortmund, Germany
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Identifiers:URI:http://www.jbc.org/cgi/content/full/278/12/10328?m... [Fulltext HTML]
URI:http://www.jbc.org/cgi/content/abstract/278/12/103... [Abstract HTML]
URI:http://www.jbc.org/cgi/reprint/278/12/10328 [Fulltext PDF]
DOI:10.1074/jbc.M213094200
LOCALID:6024 [PUMA publication management ID]
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