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Baldock, Robert A 
ORCID: 0000-0002-4649-2966, Day, Matthew, Wilkinson, Oliver J, Cloney, Ross, Jeggo, Penelope A, Oliver, Antony W, Watts, Felicity Z and Pearl, Laurence H
(2015)
ATM localization and heterochromatin repair depend on direct interaction of the 53BP1-BRCT 2 domain with γH2AX.
Cell Reports, 13 (10).
pp. 2081-2089.
doi:10.1016/j.celrep.2015.10.074
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Text (Published version)
9782-Baldock-(2015)-ATM-localization-and-heterochromatin-repair.pdf - Published Version Available under License Creative Commons Attribution Non-commercial No Derivatives 4.0. Download (3MB) | Preview |
Abstract
53BP1 plays multiple roles in mammalian DNA damage repair, mediating pathway choice and facilitating DNA double-strand break repair in heterochromatin. Although it possesses a C-terminal BRCT2 domain, commonly involved in phospho-peptide binding in other proteins, initial recruitment of 53BP1 to sites of DNA damage depends on interaction with histone post-translational modifications—H4K20me2 and H2AK13/K15ub—downstream of the early γH2AX phosphorylation mark of DNA damage. We now show that, contrary to current models, the 53BP1-BRCT2 domain binds γH2AX directly, providing a third post-translational mark regulating 53BP1 function. We find that the interaction of 53BP1 with γH2AX is required for sustaining the 53BP1-dependent focal concentration of activated ATM that facilitates repair of DNA double-strand breaks in heterochromatin in G1.
| Item Type: | Article |
|---|---|
| Article Type: | Article |
| Subjects: | Q Science > Q Science (General) Q Science > QH Natural history > QH301 Biology |
| Divisions: | Schools and Research Institutes > School of Education and Science |
| Research Priority Areas: | Place, Environment and Community |
| Depositing User: | Robbie Baldock |
| Date Deposited: | 10 Jun 2021 13:45 |
| Last Modified: | 31 Aug 2023 08:58 |
| URI: | https://eprints.glos.ac.uk/id/eprint/9782 |
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