Distinct accessory roles of Arabidopsis VEL proteins in Polycomb silencing.

Distinct accessory roles of Arabidopsis VEL proteins in Polycomb silencing.
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DOI:
10.1101/gad.350814.123
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发表时间:
2023-09-01
影响因子:
10.5
通讯作者:
Dean C
Dean C
中科院分区:
生物学1区
文献类型:
--
作者:
Franco-Echevarría E;Nielsen M;Schulten A;Cheema J;Morgan TE;Bienz M;Dean C

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在这项研究中,Franco-Echevarria等人描述了拟南芥中VEL蛋白VRN 5和Polycomb抑制复合物2(PRC 2)的核心亚基之间的结构域相互作用。他们还描述了VEL蛋白,VIN 3和转录抑制因子VAL 1之间的相互作用,共同扩展了我们对VEL辅助蛋白的个体功能及其在PRC 2组装中的作用的理解。多梳阻遏复合物2(PRC 2)介导动物和植物中靶基因的表观遗传沉默。在拟南芥中,PRC 2是FLC花阻遏基因座的冷诱导的表观遗传沉默所必需的,以使开花与春天一致。在此过程中,PRC 2依赖于VEL辅助因子,包括组成型表达的VRN 5和冷诱导的VIN 3。VEL蛋白与PRC 2在物理上相关,但它们各自的功能仍不清楚。在这里,我们显示了重组VRN 5和多个组件在一个重建的PRC 2之间的紧密联系,依赖于一个紧凑的构象VRN 5的中央结构域。介导这种紧凑构象的关键残基在整个植物界的VRN 5直系同源物中是保守的。相反,VIN 3与VAL 1相互作用,VAL 1是一种直接结合FLC的转录抑制因子。这些关联不同地影响它们在H3 K27 me沉积中的作用:这两种蛋白质都是H3 K27 me 3所必需的,但只有VRN 5是H3 K27 me 2所必需的。虽然最初被定义为春化调节因子,但VIN 3和VRN 5与拟南芥基因组中被H3 K27 me 3修饰的许多靶标共缔合。因此,我们的工作揭示了VEL蛋白在赋予FLC冷诱导沉默中的独特辅助作用,通常与PRC 2靶点具有广泛的相关性。
In this study, Franco-Echevarria et al. describe the domain interactions between VEL protein, VRN5, and the core subunits of the Polycomb repressive complex 2 (PRC2) in Arabidopsis. They also describe the interactions between VEL protein, VIN3, and the transcriptional repressor VAL1, altogether expanding our understanding of the individual functions of VEL accessory proteins and their role in PRC2 assembly on chromatin for transcriptionally repressive histone methylation. 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.
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