7F5M

Crystal structure of Sas5 YEATS domain in complex with H3K27bz peptide

7F5M の概要

• エントリーDOI: 10.2210/pdb7f5m/pdb
• 分子名称: Something about silencing protein 5, LYS-GLN-LEU-ALA-SER-LYS-ALA-ALA-ARG-LBZ-SER-ALA-PRO-SER-THR-GLY-GLY-VAL-LYS-TYR, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: histone modification, histone benzoylation, protein-protein interaction, yeats domain, 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: 3
• 化学式量合計: 35277.98

構造登録者

Wang, D.,Yan, F.,Chen, Y. (登録日: 2021-06-22, 公開日: 2022-03-16, 最終更新日: 2023-11-29)

主引用文献

Wang, D.,Yan, F.,Wu, P.,Ge, K.,Li, M.,Li, T.,Gao, Y.,Peng, C.,Chen, Y.
Global profiling of regulatory elements in the histone benzoylation pathway.
Nat Commun, 13:1369-1369, 2022

PubMed Abstract: Lysine benzoylation (Kbz) is a recently discovered post-translational modification associated with active transcription. However, the proteins for maintaining and interpreting Kbz and the physiological roles of Kbz remain elusive. Here, we systematically characterize writer, eraser, and reader proteins of histone Kbz in S. cerevisiae using proteomic, biochemical, and structural approaches. Our study identifies 27 Kbz sites on yeast histones that can be regulated by cellular metabolic states. The Spt-Ada-Gcn5 acetyltransferase (SAGA) complex and NAD-dependent histone deacetylase Hst2 could function as the writer and eraser of histone Kbz, respectively. Crystal structures of Hst2 complexes reveal the molecular basis for Kbz recognition and catalysis by Hst2. In addition, we demonstrate that a subset of YEATS domains and bromodomains serve as Kbz readers, and structural analyses reveal how YEATS and bromodomains recognize Kbz marks. Moreover, the proteome-wide screening of Kbz-modified proteins identifies 207 Kbz sites on 149 non-histone proteins enriched in ribosome biogenesis, glycolysis/gluconeogenesis, and rRNA processing pathways. Our studies identify regulatory elements for the Kbz pathway and provide a framework for dissecting the biological functions of lysine benzoylation.

PubMed: 35296687
DOI: 10.1038/s41467-022-29057-2

実験手法

X-RAY DIFFRACTION (2.4 Å)