PXD022239-1

PXD022239 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2020-10-29 02:40:14	ID requested
⏵ 1	2021-05-28 06:24:00	announced

Dataset with its publication pending

submitter keyword: proteomics, molecular chaperones, PrfC (RF3), protein quality control, protein folding

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

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PRIDE project URI

• PRIDE
  1. PXD022239
     1. Label: PRIDE project
     2. Name: Bacterial RF3 Senses Chaperone Function in Co-translational Folding