Dynamic chromatin tethering of MDC1 regulates genome stability

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ID: 328014
2026
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Abstract
DNA double-strand breaks (DSBs) are highly cytotoxic DNA lesions because they disrupt the connectivity of the DNA strand. Homologous recombination (HR) is a high-fidelity DSB repair pathway that copies the sequence spanning the break from a homologous template, but how DNA ends are held together during HR remains unclear. Here we demonstrate that the proline-serine-threonine (PST) repeat region of Mediator of DNA Damage Checkpoint 1 (MDC1) is a multivalent nucleosome-binding domain, sufficient to tether chromatin in multiple contexts. In interphase, the constitutive chromatin association of MDC1 is critical for RAD51 loading and efficient HR. In mitosis, PST-mediated chromatin binding is attenuated by phosphorylation, preventing aberrant chromosomal interactions while preserving DNA tethering by the MDC1-TOPBP1-CIP2A complex. In total, this work demonstrates that the PST repeat region of MDC1 is a multivalent nucleosome-binding domain with tunable affinity that supports DSB repair by HR and maintains genome stability during mitosis.
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openalex_W7211896659 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Joshua Heyza, Mariia Mikhova, Cody Phillips, Shomaila Mehmood, Gloria I. Perez, David Broadbent, Jens C. Schmidt
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Journal Nucleic Acids Research
Year 2026
DOI
10.1093/nar/gkag866
URL
https://doi.org/10.1093/nar/gkag866
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