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SNM1A is crucial for efficient repair of complex DNA breaks in human cells

Abstract:
DNA double-strand breaks (DSBs), such as those produced by radiation and radiomimetics, are amongst the most toxic forms of cellular damage, in part because they involve extensive oxidative modifications at the break termini. Prior to completion of DSB repair, the chemically modified termini must be removed. Various DNA processing enzymes have been implicated in the processing of these dirty ends, but molecular knowledge of this process is limited. Here, we demonstrate a role for the metallo-β-lactamase fold 5′−3′ exonuclease SNM1A in this vital process. Cells disrupted for SNM1A manifest increased sensitivity to radiation and radiomimetic agents and show defects in DSB damage repair. SNM1A is recruited and is retained at the sites of DSB damage via the concerted action of its three highly conserved PBZ, PIP box and UBZ interaction domains, which mediate interactions with poly-ADP-ribose chains, PCNA and the ubiquitinated form of PCNA, respectively. SNM1A can resect DNA containing oxidative lesions induced by radiation damage at break termini. The combined results reveal a crucial role for SNM1A to digest chemically modified DNA during the repair of DSBs and imply that the catalytic domain of SNM1A is an attractive target for potentiation of radiotherapy.
Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1038/s41467-024-49583-5

Authors


More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
RDM
Sub department:
Weatherall Insti. of Molecular Medicine
Research group:
Wolfson Imaging Centre
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Research group:
MRC-Weatherall Institute of Molecular Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Research group:
MRC-Weatherall Institute of Molecular Medicine
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MSD
Department:
Oncology
Research group:
MRC-Weatherall Institute of Molecular Medicine
Role:
Author


Publisher:
Springer Nature
Journal:
Nature Communications More from this journal
Volume:
15
Issue:
1
Article number:
5392
Publication date:
2024-06-25
Acceptance date:
2024-06-11
DOI:
EISSN:
2041-1723
ISSN:
2041-1723


Language:
English
Pubs id:
2012690
Local pid:
pubs:2012690
Deposit date:
2024-07-04

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