Arginine methylation and ubiquitylation crosstalk controls DNA end-resection and homologous recombination repair

Maria Pilar Sanchez-Bailon, Soo-Youn Choi, Elizabeth R. Dufficy, Karan Sharma, Gavin S. McNee, Emma Gunnell, Kelly Chiang, Debashish Sahay, Sarah Maslen, Grant S. Stewart, J. Mark Skehel, Ingrid Dreveny and Clare C. Davies ()
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Maria Pilar Sanchez-Bailon: University of Birmingham
Soo-Youn Choi: University of Birmingham
Elizabeth R. Dufficy: University of Birmingham
Karan Sharma: University of Birmingham
Gavin S. McNee: University of Birmingham
Emma Gunnell: University of Nottingham
Kelly Chiang: University of Birmingham
Debashish Sahay: University of Birmingham
Sarah Maslen: MRC Laboratory of Molecular Biology
Grant S. Stewart: University of Birmingham
J. Mark Skehel: MRC Laboratory of Molecular Biology
Ingrid Dreveny: University of Nottingham
Clare C. Davies: University of Birmingham

Nature Communications, 2021, vol. 12, issue 1, 1-18

Abstract: Abstract Cross-talk between distinct protein post-translational modifications is critical for an effective DNA damage response. Arginine methylation plays an important role in maintaining genome stability, but how this modification integrates with other enzymatic activities is largely unknown. Here, we identify the deubiquitylating enzyme USP11 as a previously uncharacterised PRMT1 substrate, and demonstrate that the methylation of USP11 promotes DNA end-resection and the repair of DNA double strand breaks (DSB) by homologous recombination (HR), an event that is independent from another USP11-HR activity, the deubiquitylation of PALB2. We also show that PRMT1 is a ubiquitylated protein that it is targeted for deubiquitylation by USP11, which regulates the ability of PRMT1 to bind to and methylate MRE11. Taken together, our findings reveal a specific role for USP11 during the early stages of DSB repair, which is mediated through its ability to regulate the activity of the PRMT1-MRE11 pathway.

Date: 2021
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DOI: 10.1038/s41467-021-26413-6

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