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PXD054379-1

PXD054379 is an original dataset announced via ProteomeXchange.

Dataset Summary
TitleCotranslational activity of the GroEL chaperonin
DescriptionVarious proteins in the cell begin to fold during synthesis at the ribosome, many with the assistance of molecular chaperones. While the cotranslational activity of ribosome-associated chaperones and Hsp70 is frequently studied, the role of Hsp60 chaperonins during protein synthesis remains poorly understood. Here, we studied the binding of E. coli chaperonin GroEL to ribosome-nascent chain complexes (RNCs), to understand GroEL activity during nascent chain (NC) synthesis and folding. Using biochemical reconstitution, structural proteomics and electron microscopy we describe the physical architecture of GroEL:RNC and ATP/BeFx-GroEL/ES:RNC complexes. We show that GroEL engages destabilised nascent chains on the inside of its cavity via the apical domains and disordered C-terminal tails. This GroEL:RNC complex can be capped by GroES on the NC-bound ring, with GroEL but not GroEL/ES binding promoting nascent chain destabilisation. Lastly, we observe that GroEL directly competes with Hsp70 for nascent chain binding. Our findings thus show that GroEL is a versatile chaperone which in addition to its well characterised post-translational activity can affect folding of nascent chains undergoing synthesis.
HostingRepositoryPRIDE
AnnounceDate2025-10-14
AnnouncementXMLSubmission_2025-10-14_13:50:21.890.xml
DigitalObjectIdentifier
ReviewLevelPeer-reviewed dataset
DatasetOriginOriginal dataset
RepositorySupportUnsupported dataset by repository
PrimarySubmitterAlzbeta Roeselova
SpeciesList scientific name: Escherichia coli; NCBI TaxID: NEWT:562;
ModificationListmonohydroxylated residue; iodoacetamide derivatized residue
InstrumentOrbitrap Exploris 480
Dataset History
RevisionDatetimeStatusChangeLog Entry
02024-07-30 03:12:45ID requested
12025-10-14 13:50:22announced
Publication List
10.1038/S41467-025-64968-W;
Keyword List
submitter keyword: GroEL,XL-MS, RNC
Contact List
David Balchin
contact affiliationThe Francis Crick Institute
contact emaildavid.balchin@crick.ac.uk
lab head
Alzbeta Roeselova
contact affiliationFrancis Crick Institute
contact emailalzbeta.roeselova@crick.ac.uk
dataset submitter
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