PXD013955

PXD013955 is an original dataset announced via ProteomeXchange.

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

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.

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]

submitter keyword: Yeast, HSP90, HSC90

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

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/2019/08/PXD013955

PRIDE project URI

• PRIDE
  1. PXD013955
     1. Label: PRIDE project
     2. Name: The isoforms of the molecular chaperone Hsp90 from S. cerevisiae differ in structure, function and client range