PXD025314 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble |
Description | Hsp26 is a small heat shock protein (sHsp) from S. cerevisiae. It is known to be activated by dissociation of the oligomer at heat shock temperatures. We wondered whether phosphorylation regulates its activity at physiological temperatures. In Hsp26, 9 phosphorylation sites which are located in different structural elements are known. Our analysis of phospho-mimetic mutations showed that phosphorylation activates Hsp26 at permissive temperature. The cryo-EM structure of the Hsp26 40mer revealed contacts between the conserved core domain of Hsp26 and the so-called thermosensor domain in the N-terminal part of the protein, which are targeted by phosphorylation. Furthermore, the C-terminal extension, which also links subunits within the oligomer, contains several phosphorylation sites. The introduction of negative charges at these strategic positions makes regions in the N-terminal domain accessible for the binding of substrate proteins. Relieving the intrinsic inhibition via different phosphorylation sites allows the fine-tuning of chaperone activity in response to proteotoxic stresses independent of heat activation. The described weakening of domain interactions within and between subunits could be a general regulation principle of sHsps. |
HostingRepository | PRIDE |
AnnounceDate | 2021-12-17 |
AnnouncementXML | Submission_2021-12-17_13:47:17.491.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Moritz Mühlhofer |
SpeciesList | scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932; |
ModificationList | monohydroxylated residue |
Instrument | Orbitrap Fusion |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2021-04-12 06:51:53 | ID requested | |
1 | 2021-12-17 05:52:38 | announced | |
⏵ 2 | 2021-12-17 13:47:18 | announced | 2021-12-17: Updated publication reference for PubMed record(s): 34795272.
2021-12-17: Updated publication reference for DOI(s): 10.1038/S41467-021-27036-7. |
3 | 2023-11-14 08:52:09 | announced | 2023-11-14: Updated project metadata. |
Publication List
M, ü, hlhofer M, Peters C, Kriehuber T, Kreuzeder M, Kazman P, Rodina N, Reif B, Haslbeck M, Weinkauf S, Buchner J, Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble. Nat Commun, 12(1):6697(2021) [pubmed] |
10.1038/S41467-021-27036-7; |
Keyword List
submitter keyword: Hsp26, sHsp, phosphorylation |
Contact List
Johannes Buchner |
contact affiliation | Center for Protein Assemblies, Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany |
contact email | johannes.buchner@tum.de |
lab head | |
Moritz Mühlhofer |
contact affiliation | Dept. Chemie Lichtenbergstraße 4 85748 Garching |
contact email | moritz.muehlhofer@tum.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2021/12/PXD025314 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD025314
- Label: PRIDE project
- Name: Phosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble