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Plant J. 2019 Feb;97(4):646-660. doi: 10.1111/tpj.14148. Epub 2018 Dec 18.

The Arabidopsis RRM domain protein EDM3 mediates race-specific disease resistance by controlling H3K9me2-dependent alternative polyadenylation of RPP7 immune receptor transcripts.

Author information

1
Department of Botany and Plant Sciences, Center for Plant Cell Biology, Institute of Integrative Genome Biology, University of California at Riverside, Riverside, CA, 92521, USA.
2
College of Life Sciences, Fujian Agricultural and Forestry University, Fuzhou, Fujian, 350002, China.
3
School of Life Sciences, University of Warwick, Wellesbourne Campus, Warwick, CV35 9EF, UK.
4
Biointeractions and Crop Protection, Rothamsted Research, Harpenden, AL5 2JQ, UK.
5
Department of Molecular, Cell and Systems Biology, Center for Infectious Disease and Vector Research, Institute of Integrative Genome Biology, University of California at Riverside, Riverside, CA, 92521, USA.
6
Institute of Integrative Genome Biology, University of California at Riverside, Riverside, CA, 92521, USA.
7
College of Bioresource Sciences, Nihon University, Kanagawa, 252-0880, Japan.
8
Department of Plant Pathology, Physiology, and Weed Science, Virginia Tech, Blacksburg, VA, 24060-0329, USA.

Abstract

The NLR-receptor RPP7 mediates race-specific immunity in Arabidopsis. Previous screens for enhanced downy mildew (edm) mutants identified the co-chaperone SGT1b (EDM1) and the PHD-finger protein EDM2 as critical regulators of RPP7. Here, we describe a third edm mutant compromised in RPP7 immunity, edm3. EDM3 encodes a nuclear-localized protein featuring an RNA-recognition motif. Like EDM2, EDM3 promotes histone H3 lysine 9 dimethylation (H3K9me2) at RPP7. Global profiling of H3K9me2 showed EDM3 to affect this silencing mark at a large set of loci. Importantly, both EDM3 and EDM2 co-associate in vivo with H3K9me2-marked chromatin and transcripts at a critical proximal polyadenylation site of RPP7, where they suppress proximal transcript polyadeylation/termination. Our results highlight the complexity of plant NLR gene regulation, and establish a functional and physical link between a histone mark and NLR-transcript processing.

KEYWORDS:

Hyaloperonospora arabidopsidis ; RNA-binding protein; disease-resistance genes; histone-binding proteins; transcript processing

PMID:
30407670
DOI:
10.1111/tpj.14148

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