PXD037136

PXD037136 is an original dataset announced via ProteomeXchange.

Title	Proteome dynamics at stalled replication forks reveal a coordinated recruitment of repair factors
Description	The faithful replication of DNA is a fundamental cellular process that ensures the transfer of genetic information during cell division. Genome duplication takes place during S phase and requires the dynamic and coordinated recruitment of multiple proteins at the replication forks. The instability and collapse of the replication fork can occur when cells are exposed to different genotoxic stresses, which can be overcome by the action of DNA repair pathways. Studying the proteomic interactions implicated in those events is thus a crucial step in understanding the complex biological mechanisms involved in DNA replication and repair. Proximity-dependent biotinylation coupled with mass spectrometry identification of proteins (BioID2) was used on 17 proteins from four different complexes known to play a role during DNA replication and repair to study the assembly and recruitment of proteins at stalled replication forks caused by treatment with hydroxyurea. This analysis revealed a vast interaction network of 108 proteins modulated in the presence of hydroxyurea; 45 being enriched and 63 depleted. Interestingly, 11 of them were found to be both enriched and depleted depending on the complex considered, suggesting a dynamic reorganization of the players and their interactions (?). Furthermore, the analysis identified several poorly characterized proteins, thus uncovering new players in the cellular response to DNA replication arrest. Overall, this collection of replication fork proteomes enables large-scale identification of the mechanisms of assembly and disassembly of protein complexes at the sites of stalled replication forks and provides a new framework to understand how cells respond to obstacles on DNA template, causing fork stalling or collapse.
HostingRepository	PRIDE
AnnounceDate	2026-02-06
AnnouncementXML	Submission_2026-02-05_19:15:54.735.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Dominique Levesque
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: NEWT:9606;
ModificationList	carbamoylated residue; acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	maXis

Revision	Datetime	Status	ChangeLog Entry
0	2022-10-02 04:01:42	ID requested
⏵ 1	2026-02-05 19:15:55	announced

10.1016/J.MCPRO.2024.100767;

submitter keyword: Replication fork, proteomics, DNA repair, hydroxyurea, BioID, biotinylation, interactome, DNA replication

François-Michel Boisvert
contact affiliation	Department of Immunology and Cell Biology, Faculty of Medicine and Health Sciences, Université de Sherbrooke
contact email	francois.michel.boisvert@usherbrooke.ca
lab head
Dominique Levesque
contact affiliation	University of Sherbrooke, FM Boisvert lab
contact email	dominique.levesque@usherbrooke.ca
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/02/PXD037136

PRIDE project URI

• PRIDE
  1. PXD037136
     1. Label: PRIDE project
     2. Name: Proteome dynamics at stalled replication forks reveal a coordinated recruitment of repair factors