ATM Localization and Heterochromatin Repair Depend on Direct Interaction of the 53BP1-BRCT 2 Domain with γH2AX

• DOI: 10.1016/j.celrep.2015.10.074
• Publication Date: 2015-11-25T17:47:41Z
• Authors: Robert A. Baldock; Matthew Day; Oliver J. Wilkinson; Ross Cloney; Penelope A. Jeggo; Antony W. Oliver; Felicity Z. Watts; Laurence H. Pearl
• Keywords: Heterochromatin protein 1

53BP1 plays multiple roles in mammalian DNA damage repair, mediating pathway choice and facilitating double-strand break repair heterochromatin. Although it possesses a C-terminal BRCT2 domain, commonly involved phospho-peptide binding other proteins, initial recruitment of to sites depends on interaction with histone post-translational modifications—H4K20me2 H2AK13/K15ub—downstream the early γH2AX phosphorylation mark damage. We now show that, contrary current models, 53BP1-BRCT2 domain binds directly, providing third regulating function. find that is required for sustaining 53BP1-dependent focal concentration activated ATM facilitates breaks heterochromatin G1.