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PXD025314-2

PXD025314 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitlePhosphorylation activates the yeast small heat shock protein Hsp26 by weakening domain contacts in the oligomer ensemble
DescriptionHsp26 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.
HostingRepositoryPRIDE
AnnounceDate2021-12-17
AnnouncementXMLSubmission_2021-12-17_13:47:17.491.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterMoritz Mühlhofer
SpeciesList scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationListmonohydroxylated residue
InstrumentOrbitrap Fusion
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-04-12 06:51:53ID requested
12021-12-17 05:52:38announced
22021-12-17 13:47:18announced2021-12-17: Updated publication reference for PubMed record(s): 34795272.
2021-12-17: Updated publication reference for DOI(s): 10.1038/S41467-021-27036-7.
32023-11-14 08:52:09announced2023-11-14: 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 affiliationCenter for Protein Assemblies, Department of Chemistry, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany
contact emailjohannes.buchner@tum.de
lab head
Moritz Mühlhofer
contact affiliationDept. Chemie Lichtenbergstraße 4 85748 Garching
contact emailmoritz.muehlhofer@tum.de
dataset submitter
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Dataset FTP location
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