PXD027413

PXD027413 is an original dataset announced via ProteomeXchange.

Title	A direct interplay between the co-chaperones Hop and p23 regulates cycle progression and client folding in the Hsp70/Hsp90 chaperone machineries
Description	Folding of stringent clients requires transfer from Hsp70 to Hsp90. The co-chaperone Hop physically connects the chaperone machineries. Here we define its role from the remodeling of Hsp70/40-client complexes to the mechanism of client transfer and the conformational switching from stalled to active client-processing states of Hsp90. We show that Hsp70 together with Hsp40 completely unfolds a stringent client, the glucocorticoid receptor ligand binding domain (GR-LBD) in large assemblies. Hop remodels these for efficient transfer onto Hsp90. As p23 enters, Hsp70 leaves the complex via switching between binding sites in Hop. To proceed to client folding, current concepts assume that Hop dissociates and the co-chaperone p23 stabilizes the Hsp90 closed state. In contrast, we show that p23 directly interacts with Hop, relieves the stalling Hsp90-Hop interaction and closes Hsp90. This reaction allows folding of the client and is thus the key regulatory step for the progression of the chaperone cycle. To study the interaction between the different proteins, especially p23 and the DP2 domain of Hop, we performed crosslinking-MS.
HostingRepository	PRIDE
AnnounceDate	2022-02-24
AnnouncementXML	Submission_2022-02-24_15:23:32.058.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Moritz Mühlhofer
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606; scientific name: Saccharomyces cerevisiae (Baker's yeast); NCBI TaxID: 4932;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2021-07-19 05:30:02	ID requested
⏵ 1	2022-02-24 15:23:32	announced

Dataset with its publication pending

submitter keyword: Hsp90, Hsp70, p23, Hop

Johannes Buchner
contact affiliation	Center for Protein Assemblies, Department of Chemistry, Technische Universität München, Ernst-Otto-Fischer Str. 8, 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

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PRIDE project URI

• PRIDE
  1. PXD027413
     1. Label: PRIDE project
     2. Name: A direct interplay between the co-chaperones Hop and p23 regulates cycle progression and client folding in the Hsp70/Hsp90 chaperone machineries