Distinct accessory roles of Arabidopsis VEL proteins in Polycomb silencing.

Autor:	Franco-Echevarría E; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom., Nielsen M; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom., Schulten A; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom., Cheema J; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom., Morgan TE; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom., Bienz M; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; caroline.dean@jic.ac.uk mb2@mrc-lmb.cam.ac.uk., Dean C; Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; caroline.dean@jic.ac.uk mb2@mrc-lmb.cam.ac.uk.; John Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Jazyk:	angličtina
Zdroj:	Genes & development [Genes Dev] 2023 Sep 01; Vol. 37 (17-18), pp. 801-817. Date of Electronic Publication: 2023 Sep 21.
DOI:	10.1101/gad.350814.123
Abstrakt:	Polycomb repressive complex 2 (PRC2) mediates epigenetic silencing of target genes in animals and plants. In Arabidopsis , PRC2 is required for the cold-induced epigenetic silencing of the FLC floral repressor locus to align flowering with spring. During this process, PRC2 relies on VEL accessory factors, including the constitutively expressed VRN5 and the cold-induced VIN3. The VEL proteins are physically associated with PRC2, but their individual functions remain unclear. Here, we show an intimate association between recombinant VRN5 and multiple components within a reconstituted PRC2, dependent on a compact conformation of VRN5 central domains. Key residues mediating this compact conformation are conserved among VRN5 orthologs across the plant kingdom. In contrast, VIN3 interacts with VAL1, a transcriptional repressor that binds directly to FLC These associations differentially affect their role in H3K27me deposition: Both proteins are required for H3K27me3, but only VRN5 is necessary for H3K27me2. Although originally defined as vernalization regulators, VIN3 and VRN5 coassociate with many targets in the Arabidopsis genome that are modified with H3K27me3. Our work therefore reveals the distinct accessory roles for VEL proteins in conferring cold-induced silencing on FLC , with broad relevance for PRC2 targets generally. (© 2023 Franco-Echevarría et al.; Published by Cold Spring Harbor Laboratory Press.)
Databáze:	MEDLINE
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