PXD013955 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | The isoforms of the molecular chaperone Hsp90 from S. cerevisiae differ in structure, function and client range |
Description | 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. 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 |
HostingRepository | PRIDE |
AnnounceDate | 2024-10-22 |
AnnouncementXML | Submission_2024-10-22_04:54:57.722.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Frank Stein |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | TMT6plex-126 reporter+balance reagent acylated residue |
Instrument | Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-05-21 06:51:52 | ID requested | |
1 | 2019-08-12 07:43:02 | announced | |
⏵ 2 | 2024-10-22 04:54:58 | announced | 2024-10-22: 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 affiliation | Center for Integrated Protein Science at the Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85748 Garching, Germany |
contact email | johannes.buchner@tum.de |
lab head | |
Frank Stein |
contact affiliation | EMBL |
contact email | frank.stein@embl.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD013955
- Label: PRIDE project
- Name: The isoforms of the molecular chaperone Hsp90 from S. cerevisiae differ in structure, function and client range