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Arabidopsis AGDP1 links H3K9me2 to DNA methylation in heterochromatin

Heterochromatin is a tightly packed form of chromatin that is associated with DNA methylation and histone 3 lysine 9 methylation (H3K9me). Here, we identify an H3K9me2-binding protein, Agenet domain (AGD)-containing p1 (AGDP1), in Arabidopsis thaliana. Here we find that AGDP1 can specifically recogn...

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Detalles Bibliográficos
Autores principales: Zhang, Cuijun, Du, Xuan, Tang, Kai, Yang, Zhenlin, Pan, Li, Zhu, Peipei, Luo, Jinyan, Jiang, Yuwei, Zhang, Hui, Wan, Huafang, Wang, Xingang, Wu, Fengkai, Tao, W. Andy, He, Xin-Jian, Zhang, Heng, Bressan, Ray A., Du, Jiamu, Zhu, Jian-Kang
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6208443/
https://www.ncbi.nlm.nih.gov/pubmed/30382101
http://dx.doi.org/10.1038/s41467-018-06965-w
Descripción
Sumario:Heterochromatin is a tightly packed form of chromatin that is associated with DNA methylation and histone 3 lysine 9 methylation (H3K9me). Here, we identify an H3K9me2-binding protein, Agenet domain (AGD)-containing p1 (AGDP1), in Arabidopsis thaliana. Here we find that AGDP1 can specifically recognize the H3K9me2 mark by its three pairs of tandem AGDs. We determine the crystal structure of the Agenet domain 1 and 2 cassette (AGD12) of Raphanus sativus AGDP1 in complex with an H3K9me2 peptide. In the complex, the histone peptide adopts a unique helical conformation. AGD12 specifically recognizes the H3K4me0 and H3K9me2 marks by hydrogen bonding and hydrophobic interactions. In addition, we find that AGDP1 is required for transcriptional silencing, non-CG DNA methylation, and H3K9 dimethylation at some loci. ChIP-seq data show that AGDP1 preferentially occupies long transposons and is associated with heterochromatin marks. Our findings suggest that, as a heterochromatin-binding protein, AGDP1 links H3K9me2 to DNA methylation in heterochromatin regions.