7E29

Crystal Structure of Saccharomyces cerevisiae Ioc4 PWWP domain fused with MBP

7E29 の概要

• エントリーDOI: 10.2210/pdb7e29/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose/maltodextrin-binding periplasmic protein,ISWI one complex protein 4, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: pwwp, transcription, gene regulation
• 由来する生物種: Escherichia coli (strain K12); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 61687.84

構造登録者

Li, J.,Smolle, M.,Liang, H.,Liu, Y. (登録日: 2021-02-05, 公開日: 2022-02-09, 最終更新日: 2023-11-29)

主引用文献

Li, J.,Bergmann, L.,Rafael de Almeida, A.,Webb, K.M.,Gogol, M.M.,Voigt, P.,Liu, Y.,Liang, H.,Smolle, M.M.
H3K36 methylation and DNA-binding both promote Ioc4 recruitment and Isw1b remodeler function.
Nucleic Acids Res., 50:2549-2565, 2022

PubMed Abstract: The Isw1b chromatin-remodeling complex is specifically recruited to gene bodies to help retain pre-existing histones during transcription by RNA polymerase II. Recruitment is dependent on H3K36 methylation and the Isw1b subunit Ioc4, which contains an N-terminal PWWP domain. Here, we present the crystal structure of the Ioc4-PWWP domain, including a detailed functional characterization of the domain on its own as well as in the context of full-length Ioc4 and the Isw1b remodeler. The Ioc4-PWWP domain preferentially binds H3K36me3-containing nucleosomes. Its ability to bind DNA is required for nucleosome binding. It is also furthered by the unique insertion motif present in Ioc4-PWWP. The ability to bind H3K36me3 and DNA promotes the interaction of full-length Ioc4 with nucleosomes in vitro and they are necessary for its recruitment to gene bodies in vivo. Furthermore, a fully functional Ioc4-PWWP domain promotes efficient remodeling by Isw1b and the maintenance of ordered chromatin in vivo, thereby preventing the production of non-coding RNAs.

PubMed: 35188579
DOI: 10.1093/nar/gkac077

実験手法

X-RAY DIFFRACTION (2.303 Å)