PXD010014

PXD010014 is an original dataset announced via ProteomeXchange.

Title	Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates preferentially by the HslUV protease
Description	Whereas in eukaryotic cells Hsp90s are extensively studied in bacteria, the function of Hsp90 (HtpG) and its functional relationship with Hsp70 (DnaK) remains unknown. To uncover physiological processes depending on HtpG and DnaK, we performed comparative quantitative proteomic analyses of insoluble and total protein fractions from unstressed wild type E. coli, and from knockout mutants ΔdnaKdnaJ (ΔKJ), ΔhtpG (ΔG) and ΔdnaKdnaJΔhtpG (ΔKJG) and compared their growth rates under heat-stress also with ΔdnaKdnaJΔhslV.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_05:23:52.360.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Manfredo Quadroni
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	iodoacetamide derivatized residue
Instrument	Orbitrap Fusion

Revision	Datetime	Status	ChangeLog Entry
0	2018-06-04 02:15:09	ID requested
1	2021-07-07 05:59:08	announced
2	2021-07-07 21:28:54	announced	2021-07-08: Updated publication reference for PubMed record(s): 33937334.
⏵ 3	2024-10-22 05:23:53	announced	2024-10-22: Updated project metadata.

10.3389/fmolb.2021.653073;

Fauvet B, Finka A, Castani, é, -Cornet MP, Cirinesi AM, Genevaux P, Quadroni M, Goloubinoff P, Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70-Hsp40 Substrates. Front Mol Biosci, 8():653073(2021) [pubmed]

curator keyword: Biological

submitter keyword: DnaJ, HslV,DnaK, HtpG, proteostasis

Pierre Goloubinoff
contact affiliation	University of Lausanne Department of Plant Molecular Biology (DBMV) UNIL-Sorge, Biophore Building CH-1015 Lausanne Switzerland
contact email	Pierre.Goloubinoff@unil.ch
lab head
Manfredo Quadroni
contact affiliation	University of Lausanne
contact email	manfredo.quadroni@unil.ch
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/2021/07/PXD010014

PRIDE project URI

• PRIDE
  1. PXD010014
     1. Label: PRIDE project
     2. Name: Bacterial Hsp90 mediates the degradation of aggregation-prone Hsp70-Hsp40 substrates preferentially by the HslUV protease