H3K4me1 recruits DNA repair proteins in plants.

Autor:	Quiroz D; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA.; Integrative Genetics and Genomics, University of California Davis, Davis, CA 95616, USA., Oya S; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA.; Laboratory of Genetics, Department of Biological Sciences, The University of Tokyo, Tokyo 113-0033, Japan., Lopez-Mateos D; Department of Physiology and Membrane Biology, University of California Davis, Davis, CA 95616, USA.; Biophysics Graduate Group, University of California Davis, Davis, CA 95616, USA., Zhao K; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA.; Plant Biology Graduate Group, University of California Davis, Davis, CA 95616, USA., Pierce A; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA.; Plant Biology Graduate Group, University of California Davis, Davis, CA 95616, USA., Ortega L; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA., Ali A; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA., Carbonell-Bejerano P; Instituto de Ciencias de la Vid y del Vino (ICVV, CSIC-CAR-UR), Logroño 26007, La Rioja, Spain., Yarov-Yarovoy V; Department of Physiology and Membrane Biology, University of California Davis, Davis, CA 95616, USA.; Biophysics Graduate Group, University of California Davis, Davis, CA 95616, USA., Suzuki S; Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya 464-0814, Japan., Hayashi G; Department of Biomolecular Engineering, Graduate School of Engineering, Nagoya University, Nagoya 464-0814, Japan., Osakabe A; Laboratory of Genetics, Department of Biological Sciences, The University of Tokyo, Tokyo 113-0033, Japan.; PRESTO, Japan Science and Technology Agency, Kawaguchi 332-0012, Japan., Monroe G; Department of Plant Sciences, University of California Davis, Davis, CA 95616, USA.; Integrative Genetics and Genomics, University of California Davis, Davis, CA 95616, USA.; Plant Biology Graduate Group, University of California Davis, Davis, CA 95616, USA.
Jazyk:	angličtina
Zdroj:	The Plant cell [Plant Cell] 2024 May 29; Vol. 36 (6), pp. 2410-2426.
DOI:	10.1093/plcell/koae089
Abstrakt:	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. Competing Interests: Conflict of interest statement. None declared. (© The Author(s) 2024. Published by Oxford University Press on behalf of American Society of Plant Biologists. All rights reserved. For commercial re-use, please contact reprints@oup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.)
Databáze:	MEDLINE
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