| Literature DB >> 25417107 |
Yuanyuan Li1, Hong Wen2, Yuanxin Xi3, Kaori Tanaka4, Haibo Wang5, Danni Peng6, Yongfeng Ren5, Qihuang Jin6, Sharon Y R Dent7, Wei Li3, Haitao Li8, Xiaobing Shi9.
Abstract
The recognition of modified histones by "reader" proteins constitutes a key mechanism regulating gene expression in the chromatin context. Compared with the great variety of readers for histone methylation, few protein modules that recognize histone acetylation are known. Here, we show that the AF9 YEATS domain binds strongly to histone H3K9 acetylation and, to a lesser extent, H3K27 and H3K18 acetylation. Crystal structural studies revealed that AF9 YEATS adopts an eight-stranded immunoglobin fold and utilizes a serine-lined aromatic "sandwiching" cage for acetyllysine readout, representing a novel recognition mechanism that is distinct from that of known acetyllysine readers. ChIP-seq experiments revealed a strong colocalization of AF9 and H3K9 acetylation genome-wide, which is important for the chromatin recruitment of the H3K79 methyltransferase DOT1L. Together, our studies identified the evolutionarily conserved YEATS domain as a novel acetyllysine-binding module and established a direct link between histone acetylation and DOT1L-mediated H3K79 methylation in transcription control.Entities:
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Year: 2014 PMID： 25417107 PMCID： PMC4344132 DOI： 10.1016/j.cell.2014.09.049
Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582