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PXD013955

PXD013955 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe isoforms of the molecular chaperone Hsp90 from S. cerevisiae differ in structure, function and client range
DescriptionThe 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. Hspc82 and Hsc82 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 conditions and heat shock. 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
HostingRepositoryPRIDE
AnnounceDate2024-10-22
AnnouncementXMLSubmission_2024-10-22_04:54:57.722.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterFrank Stein
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListTMT6plex-126 reporter+balance reagent acylated residue
InstrumentQ Exactive Plus
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-05-21 06:51:52ID requested
12019-08-12 07:43:02announced
22024-10-22 04:54:58announced2024-10-22: Updated project metadata.
Publication List
10.1038/s41467-019-11518-w;
Girstmair H, Tippel F, Lopez A, Tych K, Stein F, Haberkant P, Schmid PWN, Helm D, Rief M, Sattler M, Buchner J, The Hsp90 isoforms from S. cerevisiae differ in structure, function and client range. Nat Commun, 10(1):3626(2019) [pubmed]
Keyword List
submitter keyword: Yeast, HSP90, HSC90
Contact List
Johannes Buchner
contact affiliationCenter for Integrated Protein Science at the Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany
contact emailjohannes.buchner@tum.de
lab head
Frank Stein
contact affiliationEMBL
contact emailfrank.stein@embl.de
dataset submitter
Full Dataset Link List
Dataset FTP location
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PRIDE project URI
Repository Record List
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