PXD048623-1

PXD048623 is an original dataset announced via ProteomeXchange.

Title	Mechanism of chaperone coordination during cotranslational protein folding in bacteria
Description	Protein folding is assisted by molecular chaperones that bind nascent polypeptides during mRNA translation. Several structurally-distinct classes of chaperone promote de novo folding, suggesting that their activities are coordinated at the ribosome. We used biochemical reconstitution and structural proteomics to explore the molecular basis for cotranslational chaperone action in bacteria. We found that chaperone binding is disfavoured close to the ribosome, allowing folding to precede chaperone recruitment. Trigger factor recognises compact folding intermediates exposing extensive unfolded surface and dictates DnaJ access to nascent chains. DnaJ uses a large surface to bind structurally diverse intermediates, and recruits DnaK to sequence-diverse solvent-accessible sites. Neither Trigger factor, DnaJ nor DnaK destabilize cotranslational folding intermediates. Instead, the chaperones collaborate to protect incipient structure in the nascent polypeptide well beyond the ribosome exit tunnel. Our findings show how the chaperone network selects and modulates cotranslational folding intermediates.
HostingRepository	PRIDE
AnnounceDate	2024-07-03
AnnouncementXML	Submission_2024-07-03_11:53:35.992.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Alzbeta Roeselova
SpeciesList	scientific name: Escherichia coli; NCBI TaxID: 562;
ModificationList	monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Eclipse

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-16 20:00:27	ID requested
⏵ 1	2024-07-03 11:53:36	announced
2	2024-10-22 06:48:45	announced	2024-10-22: Updated project metadata.

10.1016/J.MOLCEL.2024.06.002;

submitter keyword: nascent chain, ribosomes,XL-MS, molecular chaperones, protein synthesis, β-galactosidase, protein folding

David Balchin
contact affiliation	Protein Biogenesis Laboratory, Francis Crick Institute, London, UK
contact email	david.balchin@crick.ac.uk
lab head
Alzbeta Roeselova
contact affiliation	Francis Crick Institute
contact email	alzbeta.roeselova@crick.ac.uk
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD048623
     1. Label: PRIDE project
     2. Name: Mechanism of chaperone coordination during cotranslational protein folding in bacteria