文献类型： 外文期刊
作者： Xu, Mengting 1 ; Zhang, Qi 1 ; Shi, Huanbin 2 ; Wu, Zhongling 1 ; Zhou, Wei 1 ; Lin, Fucheng 3 ; Kou, Yanjun 2 ; Tao, Zeng 1 ;
作者机构： 1.Zhejiang Univ, Inst Biotechnol, State Key Lab Rice Biol & Breeding, Key Lab Biol Crop Pathogens & Insects Zhejiang Pro, Hangzhou, Peoples R China
2.China Natl Rice Res Inst, State Key Lab Rice Biol & Breeding, Hangzhou, Peoples R China
3.Zhejiang Acad Agr Sci, Inst Plant Protect & Microbiol, State Key Lab Managing Biot & Chem Treats Qual & S, Hangzhou, Peoples R China
期刊名称：NATURE COMMUNICATIONS （ 影响因子：14.7； 五年影响因子：16.1 ）
ISSN：
年卷期： 2024 年 15 卷 1 期
页码：
收录情况： SCI
摘要： In animals, evolutionarily conserved Polycomb repressive complex 2 (PRC2) catalyzes histone H3 lysine 27 trimethylation (H3K27me3) and PRC1 functions in recruitment and transcriptional repression. However, the mechanisms underlying H3K27me3-mediated stable transcriptional silencing are largely unknown, as PRC1 subunits are poorly characterized in fungi. Here, we report that in the filamentous fungus Magnaporthe oryzae, the N-terminal chromodomain and C-terminal MRG domain of Eaf3 play key roles in facultative heterochromatin formation and transcriptional silencing. Eaf3 physically interacts with Ash1, Eed, and Sin3, encoding an H3K36 methyltransferase, the core subunit of PRC2, and a histone deacetylation co-suppressor, respectively. Eaf3 co-localizes with a set of repressive Ash1-H3K36me2 and H3K27me3 loci and mediates their transcriptional silencing. Furthermore, Eaf3 acts as a histone reader for the repressive H3K36me2 and H3K27me3 marks. Eaf3-occupied regions are associated with increased nucleosome occupancy, contributing to transcriptional silencing in M. oryzae. Together, these findings reveal that Eaf3 is a repressive H3K36me2 reader and plays a vital role in Polycomb gene silencing and the formation of facultative heterochromatin in fungi. The authors characterize a repressive H3K36me2 reader that plays a PRC1-like role in Polycomb gene silencing and facultative heterochromatin formation in fungi that functions through direct interaction with a PRC2 subunit, a histone deacetylation co-suppressor, and nucleosome compaction.
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