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Plant HP1 protein ADCP1 links multivalent H3K9 methylation readout to heterochromatin formation

Heterochromatin Protein 1 (HP1) recognizes histone H3 lysine 9 methylation (H3K9me) through its conserved chromodomain and maintains heterochromatin from fission yeast to mammals. However, in Arabidopsis , Like Heterochromatin Protein 1 (LHP1) recognizes and colocalizes genome-wide with H3K27me3, an...

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Published in:Cell research 2019-01, Vol.29 (1), p.54-66
Main Authors: Zhao, Shuai, Cheng, Lingling, Gao, Yifei, Zhang, Baichao, Zheng, Xiangdong, Wang, Liang, Li, Pilong, Sun, Qianwen, Li, Haitao
Format: Article
Language:English
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Summary:Heterochromatin Protein 1 (HP1) recognizes histone H3 lysine 9 methylation (H3K9me) through its conserved chromodomain and maintains heterochromatin from fission yeast to mammals. However, in Arabidopsis , Like Heterochromatin Protein 1 (LHP1) recognizes and colocalizes genome-wide with H3K27me3, and is the functional homolog of Polycomb protein. This raises the question whether genuine HP1 homologs exist in plants. Here, we report on the discovery of ADCP1, a plant-specific triple tandem Agenet protein, as a multivalent H3K9me reader in Arabidopsis , and establish that ADCP1 is essential for heterochromatin formation and transposon silencing through modulating H3K9 and DNA methylation levels. Structural studies revealed the molecular basis underlying H3K9me-specific recognition by tandem Agenet of ADCP1. Similar to human HP1α and fly HP1a, ADCP1 mediates heterochromatin phase separation. Our results demonstrate that despite its distinct domain compositions, ADCP1 convergently evolves as an HP1-equivalent protein in plants to regulate heterochromatin formation.
ISSN:1001-0602
1748-7838
DOI:10.1038/s41422-018-0104-9