The Arabidopsis acetylated histone-binding protein BRAT1 forms a complex with BRP1 and prevents transcriptional silencing

Cui-Jun Zhang, Xiao-Mei Hou, Lian-Mei Tan, Chang-Rong Shao, Huan-Wei Huang, Yong-Qiang Li, Lin Li, Tao Cai, She Chen and Xin-Jian He ()
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Cui-Jun Zhang: National Institute of Biological Sciences
Xiao-Mei Hou: National Institute of Biological Sciences
Lian-Mei Tan: National Institute of Biological Sciences
Chang-Rong Shao: National Institute of Biological Sciences
Huan-Wei Huang: National Institute of Biological Sciences
Yong-Qiang Li: National Institute of Biological Sciences
Lin Li: National Institute of Biological Sciences
Tao Cai: National Institute of Biological Sciences
She Chen: National Institute of Biological Sciences
Xin-Jian He: National Institute of Biological Sciences

Nature Communications, 2016, vol. 7, issue 1, 1-13

Abstract: Abstract Transposable elements and other repetitive DNA sequences are usually subject to DNA methylation and transcriptional silencing. However, anti-silencing mechanisms that promote transcription in these regions are not well understood. Here, we describe an anti-silencing factor, Bromodomain and ATPase domain-containing protein 1 (BRAT1), which we identified by a genetic screen in Arabidopsis thaliana. BRAT1 interacts with an ATPase domain-containing protein, BRP1 (BRAT1 Partner 1), and both prevent transcriptional silencing at methylated genomic regions. Although BRAT1 mediates DNA demethylation at a small set of loci targeted by the 5-methylcytosine DNA glycosylase ROS1, the involvement of BRAT1 in anti-silencing is largely independent of DNA demethylation. We also demonstrate that the bromodomain of BRAT1 binds to acetylated histone, which may facilitate the prevention of transcriptional silencing. Thus, BRAT1 represents a potential link between histone acetylation and transcriptional anti-silencing at methylated genomic regions, which may be conserved in eukaryotes.

Date: 2016
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DOI: 10.1038/ncomms11715

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