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PXD012929-1

PXD012929 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleThe Hsp70 Chaperone System Stabilizes a Thermo-sensitive Subproteome
DescriptionStress-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).
HostingRepositoryPRIDE
AnnounceDate2019-06-24
AnnouncementXMLSubmission_2019-06-24_05:43:36.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterLiang Zhao
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListNo PTMs are included in the dataset
InstrumentQ Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02019-03-01 03:51:53ID requested
12019-06-24 05:43:37announced
22019-08-08 03:21:46announcedUpdated publication reference for PubMed record(s): 31365874.
Publication List
Dataset with its publication pending
Keyword List
curator keyword: Biological
submitter keyword: Chaperones, pulse proteolysis, proteomics, protein stability,
Contact List
Liang Zhao
contact affiliationDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
contact emailzhao@biochem.mpg.de
lab head
Liang Zhao
contact affiliationMax Planck Institute of Biochemistry
contact emailzhao@biochem.mpg.de
dataset submitter
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Dataset FTP location
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