Journal ArticleH3K4me1 recruits DNA repair proteins in plantsQuiroz, Daniela; Oya, Satoyo; Lopez-Mateos, Diego; Zhao, Kehan; Pierce, Alice; Ortega, Lissandro; Ali, Alissza; Carbonell-Bejerano, Pablo; Yarov-Yarovoy, Vladimir; Suzuki, Sae; Hayashi, Gosuke; Osakabe, Akihisa; Monroe, Grey<title>Abstract</title> <p>DNA repair proteins can be recruited by their histone reader domains to specific epigenomic features, with consequences on intragenomic mutation rate variation. Here, we investigated H3K4me1-associated hypomutation in plants. We first examined 2 proteins which, in plants, contain Tudor histone reader domains: PRECOCIOUS DISSOCIATION OF SISTERS 5 (PDS5C), involved in homology-directed repair, and MUTS HOMOLOG 6 (MSH6), a mismatch repair protein. The MSH6 Tudor domain of Arabidopsis (Arabidopsis thaliana) binds to H3K4me1 as previously demonstrated for PDS5C, which localizes to H3K4me1-rich gene bodies and essential genes. Mutations revealed by ultradeep sequencing of wild-type and msh6 knockout lines in Arabidopsis show that functional MSH6 is critical for the reduced rate of single-base substitution (SBS) mutations in gene bodies and H3K4me1-rich regions. We explored the breadth of these mechanisms among plants by examining a large rice (Oryza sativa) mutation data set. H3K4me1-associated hypomutation is conserved in rice as are the H3K4me1-binding residues of MSH6 and PDS5C Tudor domains. Recruitment of DNA repair proteins by H3K4me1 in plants reveals convergent, but distinct, epigenome-recruited DNA repair mechanisms from those well described in humans. The emergent model of H3K4me1-recruited repair in plants is consistent with evolutionary theory regarding mutation modifier systems and offers mechanistic insight into intragenomic mutation rate variation in plants.</p>The Plant Cell2024-03-2610513408The Plant Cell3662410 to 24261040-4651https://doi.org/10.1093/plcell/koae0892317191National Science Foundation