5D7E

Crystal structure of Taf14 YEATS domain in complex with H3K9ac

5D7E の概要

• エントリーDOI: 10.2210/pdb5d7e/pdb
• 分子名称: Transcription initiation factor TFIID subunit 14, H3K9ac, DI(HYDROXYETHYL)ETHER, ... (5 entities in total)
• 機能のキーワード: acetylation histone yeats reader, nuclear protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17444.92

構造登録者

Andrews, F.H.,Shanle, E.K.,Strahl, B.D.,Kutateladze, T.G. (登録日: 2015-08-13, 公開日: 2015-09-23, 最終更新日: 2024-10-09)

主引用文献

Shanle, E.K.,Andrews, F.H.,Meriesh, H.,McDaniel, S.L.,Dronamraju, R.,DiFiore, J.V.,Jha, D.,Wozniak, G.G.,Bridgers, J.B.,Kerschner, J.L.,Krajewski, K.,Martin, G.M.,Morrison, A.J.,Kutateladze, T.G.,Strahl, B.D.
Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.
Genes Dev., 29:1795-1800, 2015

PubMed Abstract: The YEATS domain, found in a number of chromatin-associated proteins, has recently been shown to have the capacity to bind histone lysine acetylation. Here, we show that the YEATS domain of Taf14, a member of key transcriptional and chromatin-modifying complexes in yeast, is a selective reader of histone H3 Lys9 acetylation (H3K9ac). Structural analysis reveals that acetylated Lys9 is sandwiched in an aromatic cage formed by F62 and W81. Disruption of this binding in cells impairs gene transcription and the DNA damage response. Our findings establish a highly conserved acetyllysine reader function for the YEATS domain protein family and highlight the significance of this interaction for Taf14.

PubMed: 26341557
DOI: 10.1101/gad.269977.115

実験手法

X-RAY DIFFRACTION (1.9 Å)