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          Institute: MPI für medizinische Forschung     Collection: Jahbruch 2014_archival     Display Documents



ID: 681484.0, MPI für medizinische Forschung / Jahbruch 2014_archival
Integration of the accelerator Aha1 in the Hsp90 co−chaperone cycle
Translation of Title:Integration of the accelerator Aha1 in the Hsp90 co−chaperone cycle
Authors:Li, Jing; Richter, Klaus; Reinstein, Jochen; Buchner, Johannes
Language:English
Date of Publication (YYYY-MM-DD):2013-03-01
Title of Journal:Nature Structural and Molecular Biology
Journal Abbrev.:Nat. Struct. Mol. Biol.
Volume:20
Issue / Number:3
Start Page:326
End Page:331
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description:Heat−shock protein 90 (Hsp90) is an ATP−dependent molecular chaperone that associates dynamically with various co−chaperones during its chaperone cycle. Here we analyzed the role of the activating co−chaperone Aha1 in the progression of the yeast Hsp90 chaperone cycle and identified a critical ternary Hsp90 complex containing the co−chaperones Aha1 and Cpr6. Aha1 accelerates the intrinsically slow conformational transitions of Hsp90 to an N−terminally associated state but does not fully close the nucleotide−binding pocket yet. Cpr6 increases the affinity between Aha1 and Hsp90 and further stimulates the Hsp90 ATPase activity. Synergistically, Aha1 and Cpr6 displace the inhibitory co−chaperone Sti1 from Hsp90. To complete the cycle, Aha1 is released by the co−chaperone p23. Thus, at distinct steps during the Hsp90 chaperone cycle, co−chaperones selectively trap statistically distributed Hsp90 conformers and thus turn Hsp90 into a deterministic machine
External Publication Status:published
Document Type:Article
Communicated by:wkaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
Identifiers:LOCALID:7842
URI:http%3A%2F%2Fwww.nature.com%2Fnsmb%2Fjournal%2Fvao...
URI:http%3A%2F%2Fwww.nature.com%2Fnsmb%2Fjournal%2Fvao...
URI:http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fpubmed%2F23396...
DOI:10.1038%2Fnsmb.2502
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