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Girstmair, H.* ; Tippel, F.* ; Lopez, A. ; Tych, K.* ; Stein, F.* ; Haberkant, P.* ; Schmid, P.W.N.* ; Helm, D.* ; Rief, M.* ; Sattler, M. ; Buchner, J.*

The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range.

Nat. Commun. 10:3626 (2019)
Publ. Version/Full Text Research data DOI PMC
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The molecular chaperone Hsp90 is an important regulator of proteostasis. It has remained unclear why S. cerevisiae possesses two Hsp90 isoforms, the constitutively expressed Hsc82 and the stress-inducible Hsp82. Here, we report distinct differences despite a sequence identity of 97%. Consistent with its function under stress conditions, Hsp82 is more stable and refolds more efficiently than Hsc82. The two isoforms also differ in their ATPases and conformational cycles. Hsc82 is more processive and populates closed states to a greater extent. Variations in the N-terminal ATP-binding domain modulate its dynamics and conformational cycle. Despite these differences, the client interactomes are largely identical, but isoform-specific interactors exist both under physiological and heat shock conditions. Taken together, changes mainly in the N-domain create a stress-specific, more resilient protein with a shifted activity profile. Thus, the precise tuning of the Hsp90 isoforms preserves the basic mechanism but adapts it to specific needs.
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Publication type Article: Journal article
Document type Scientific Article
Language
Publication Year 2019
HGF-reported in Year 2019
ISSN (print) / ISBN 2041-1723
e-ISSN 2041-1723
Journal Nature Communications
Quellenangaben Volume: 10, Issue: 1, Pages: , Article Number: 3626 Supplement: ,
Publisher Nature Publishing Group
Publishing Place London
Reviewing status Peer reviewed
Institute(s) Institute of Structural Biology (STB)
POF-Topic(s) 30203 - Molecular Targets and Therapies
Research field(s) Enabling and Novel Technologies
PSP Element(s) G-503000-001
DOI 10.1038/s41467-019-11518-w
WOS ID WOS:000480234900001
Scopus ID 85070364208
PubMed ID 31399574
Erfassungsdatum 2019-08-13
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