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PXD022239

PXD022239 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleBacterial RF3 Senses Chaperone Function in Co-translational Folding
DescriptionMolecular chaperones assist in protein folding by interacting with nascent polypeptide chains (NCs) during translation, but whether the ribosome can sense chaperone defects and abort translation of misfolding NCs has not been explored. Here we used quantitative proteomics in E. coli to investigate the ribosome-associated chaperone network and the consequences of its dysfunction. Trigger factor and the DnaK (Hsp70) system are the major NC-binding chaperones. HtpG (Hsp90), GroEL and ClpB contribute increasingly, when DnaK is deficient. Surprisingly, misfolding of NCs due to defects in co-translational chaperone function or amino acid analog incorporation, results in recruitment of the non-canonical release factor RF3 to the ribosome. RF3 then cooperates with RF2 in mediating premature chain termination of a subset of abundant NCs, allowing their efficient degradation. This function of RF3 reduces the accumulation of misfolded proteins. It is critical for proteostasis maintenance and cell growth under conditions of limited chaperone availability.
HostingRepositoryPRIDE
AnnounceDate2021-05-28
AnnouncementXMLSubmission_2021-05-28_06:24:00.427.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 HF; Q Exactive
Dataset History
RevisionDatetimeStatusChangeLog Entry
02020-10-29 02:40:14ID requested
12021-05-28 06:24:00announced
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: proteomics, molecular chaperones, PrfC (RF3), protein quality control, protein folding
Contact List
Ulrich Hartl
contact affiliationDepartment of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany
contact emailuhartl@biochem.mpg.de
lab head
Liang Zhao
contact affiliationMax Planck Institute of Biochemistry
contact emailzhao@biochem.mpg.de
dataset submitter
Full Dataset Link List
Dataset FTP location
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