PXD012929

PXD012929 is an original dataset announced via ProteomeXchange.

Title	The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome
Description	Stress-inducible molecular chaperones have essential roles in maintaining protein homeostasis, but the extent to which they affect global proteome stability remains unclear. Here, we analyzed the effects of the DnaK (Hsp70) system on protein stability in Escherichia coli using pulse proteolysis combined with quantitative proteomics. We quantified ~1500 soluble proteins and found ~500 of them to be protease-sensitive under normal growth conditions, indicating a high prevalence of conformationally dynamic states. Acute heat stress resulted in unfolding of an additional ~200 proteins, reflected in exposure of otherwise buried hydrophobic regions. Overexpression of the DnaK chaperone system markedly stabilized most thermo-sensitive proteins, including numerous ribosomal proteins as well as large, hetero-oligomeric proteins that frequently contain the evolutionary ancient c.37 fold (P-loop nucleoside triphosphate hydrolases).
HostingRepository	PRIDE
AnnounceDate	2019-06-24
AnnouncementXML	Submission_2019-08-08_03:21:44.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Liang Zhao
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	No PTMs are included in the dataset
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2019-03-01 03:51:53	ID requested
1	2019-06-24 05:43:37	announced
⏵ 2	2019-08-08 03:21:46	announced	Updated publication reference for PubMed record(s): 31365874.

Zhao L, Vecchi G, Vendruscolo M, K, ö, rner R, Hayer-Hartl M, Hartl FU, coli. Cell Rep, 28(5):1335-1345.e6(2019) [pubmed]

curator keyword: Biological

submitter keyword: Chaperones, pulse proteolysis, proteomics, protein stability,

Liang Zhao
contact affiliation	Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
contact email	zhao@biochem.mpg.de
lab head
Liang Zhao
contact affiliation	Max Planck Institute of Biochemistry
contact email	zhao@biochem.mpg.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/2019/06/PXD012929

PRIDE project URI

• PRIDE
  1. PXD012929
     1. Label: PRIDE project
     2. Name: The Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome