PXD038019

PXD038019 is an original dataset announced via ProteomeXchange.

Title	The permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions
Description	Small Heat shock proteins (sHsps) are a family of molecular chaperones that bind non-native proteins in an ATP-independent manner. C. elegans encodes 16 different sHsps, among them Hsp17, which is evolutionarily distinct from other sHsps in the nematode. The structure and mechanism of Hsp17 and how these may differ from other sHsps remain unclear. Here, we find that Hsp17 has a distinct expression pattern, structural organization, and chaperone function. Consistent with its presence under non-stress conditions, and in contrast to many other sHsps, we determined that Hsp17 is a mono-disperse, permanently active chaperone in vitro, which interacts with hundreds of different C. elegans proteins under physiological conditions. Additionally, our cryo-EM structure of Hsp17 reveals that in the 24-mer complex, 12 N-terminal regions are involved in its chaperone function. These flexible regions are located on the outside of the spherical oligomer, whereas the other 12 N-terminal regions are engaged in stabilizing interactions in its interior. This allows the same region in Hsp17 to perform different functions depending on the topological context. Taken together, our results reveal structural and functional features that further define the structural basis of permanently active sHsps.
HostingRepository	PRIDE
AnnounceDate	2023-11-14
AnnouncementXML	Submission_2023-11-14_08:59:50.499.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Annika Strauch
SpeciesList	scientific name: Caenorhabditis elegans; NCBI TaxID: 6239;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2022-11-07 10:12:26	ID requested
1	2022-12-08 06:49:11	announced
⏵ 2	2023-11-14 08:59:51	announced	2023-11-14: Updated project metadata.

Dataset with its publication pending

ProteomeXchange project tag: Protein Misfolding and Aggregation (B/D-HPP), Biology/Disease-Driven Human Proteome Project (B/D-HPP), Human Proteome Project

submitter keyword: molecular chaperone, protein structure, protein aggregation, small heat shock protein

Johannes Buchner
contact affiliation	Center for Protein Assemblies and Department of Chemistry, Technische Universität München, Ernst-Otto-Fischer Strasse 8, 85748 Garching, Germany
contact email	johannes.buchner@tum.de
lab head
Annika Strauch
contact affiliation	Technical University Munich (TUM)
contact email	annika.strauch@tum.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/2022/12/PXD038019

PRIDE project URI

• PRIDE
  1. PXD038019
     1. Label: PRIDE project
     2. Name: The permanently chaperone-active small heat shock protein Hsp17 from C. elegans exhibits topological separation of its N-terminal regions