PXD048645

PXD048645 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 chaperones promote de novo folding, suggesting that their activity is coordinated at the ribosome. Here we use biochemical reconstitution and structural proteomics to explore the molecular basis for cotranslational chaperone action in bacteria. We find that chaperone binding is disfavoured close to the ribosome, allowing folding to precede chaperone recruitment. Trigger factor subsequently recognises compact folding intermediates exposing extensive non-native surface and dictates DnaJ access to nascent chains. DnaJ uses a large surface to bind structurally diverse intermediates, and recruits DnaK to solvent-accessible sites in a sequence non-specific manner. Neither Trigger factor, DnaJ nor DnaK destabilize cotranslational folding intermediates. Instead, the chaperones collaborate to create a protected space for protein maturation that extends well beyond the ribosome exit tunnel. Our findings show how the chaperone network selects and modulates cotranslational folding intermediates.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_06:48:44.096.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	acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	Orbitrap Fusion Lumos

Revision	Datetime	Status	ChangeLog Entry
0	2024-01-17 06:00:52	ID requested
1	2024-07-03 07:38:58	announced
⏵ 2	2024-10-22 06:48:44	announced	2024-10-22: Updated project metadata.

10.1016/J.MOLCEL.2024.06.002;

submitter keyword: nascent chain, ribosomes,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. PXD048645
     1. Label: PRIDE project
     2. Name: Mechanism of chaperone coordination during cotranslational protein folding in bacteria