PXD022239 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Bacterial RF3 Senses Chaperone Function in Co-translational Folding |
Description | Molecular 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. |
HostingRepository | PRIDE |
AnnounceDate | 2021-05-28 |
AnnouncementXML | Submission_2021-05-28_06:24:00.427.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 HF; Q Exactive |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2020-10-29 02:40:14 | ID requested | |
⏵ 1 | 2021-05-28 06:24:00 | announced | |
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 affiliation | Department of Cellular Biochemistry, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany |
contact email | uhartl@biochem.mpg.de |
lab head | |
Liang Zhao |
contact affiliation | Max Planck Institute of Biochemistry |
contact email | zhao@biochem.mpg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD022239
- Label: PRIDE project
- Name: Bacterial RF3 Senses Chaperone Function in Co-translational Folding