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PXD025219

PXD025219 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
AnnounceDate2023-11-14
AnnouncementXMLSubmission_2023-11-14_08:52:19.570.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterRoman Körner
SpeciesList scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationListacetylated residue; iodoacetamide derivatized residue
InstrumentQ Exactive HF
Dataset History
RevisionDatetimeStatusChangeLog Entry
02021-04-06 07:13:05ID requested
12022-12-09 07:08:16announced
22023-11-14 08:52:20announced2023-11-14: Updated project metadata.
Publication List
Dataset with its publication pending
Keyword List
submitter keyword: Molecular chaperones, co-translational folding
Contact List
F. Ulrich Hartl
contact affiliationMax-Planck Institute of Biochemistry, Department of Cellular Biochemistry
contact emailuhartl@biochem.mpg.de
lab head
Roman Körner
contact affiliationMax-Planck Institute of Biochemistry, Department of Cellular Biochemistry
contact emailrkoerner@biochem.mpg.de
dataset submitter
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Dataset FTP location
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