4TMP

Crystal structure of AF9 YEATS bound to H3K9ac peptide

4TMP の概要

• エントリーDOI: 10.2210/pdb4tmp/pdb
• 分子名称: Protein AF-9, ALA-ARG-THR-LYS-GLN-THR-ALA-ARG-ALY-SER-THR, 1,2-ETHANEDIOL, ... (4 entities in total)
• 機能のキーワード: transcription, complex, histone modification, immunoglobin fold
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 36055.52

構造登録者

Li, H.,Li, Y.,Wang, H.,Ren, Y. (登録日: 2014-06-02, 公開日: 2014-11-05, 最終更新日: 2024-11-06)

主引用文献

Li, Y.,Wen, H.,Xi, Y.,Tanaka, K.,Wang, H.,Peng, D.,Ren, Y.,Jin, Q.,Dent, S.Y.,Li, W.,Li, H.,Shi, X.
AF9 YEATS Domain Links Histone Acetylation to DOT1L-Mediated H3K79 Methylation.
Cell, 159:558-571, 2014

PubMed 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.

PubMed: 25417107
DOI: 10.1016/j.cell.2014.09.049

実験手法

X-RAY DIFFRACTION (2.3 Å)