6S01

Structure of LEDGF PWWP domain bound H3K36 methylated nucleosome

6S01 の概要

• エントリーDOI: 10.2210/pdb6s01/pdb
• EMDBエントリー: 10069
• 分子名称: Histone H3, Histone H4, Histone H2A, ... (7 entities in total)
• 機能のキーワード: ledgf, pwwp, h3k36me3, nucleosome, transcription
• 由来する生物種: Xenopus laevis (African clawed frog); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 270290.78

構造登録者

Wang, H.,Farnung, L.,Dienemann, C.,Cramer, P. (登録日: 2019-06-13, 公開日: 2019-12-18, 最終更新日: 2024-10-16)

主引用文献

Wang, H.,Farnung, L.,Dienemann, C.,Cramer, P.
Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding.
Nat.Struct.Mol.Biol., 27:8-13, 2020

PubMed Abstract: Recognition of histone-modified nucleosomes by specific reader domains underlies the regulation of chromatin-associated processes. Whereas structural studies revealed how reader domains bind modified histone peptides, it is unclear how reader domains interact with modified nucleosomes. Here, we report the cryo-electron microscopy structure of the PWWP reader domain of human transcriptional coactivator LEDGF in complex with an H3K36-methylated nucleosome at 3.2-Å resolution. The structure reveals multivalent binding of the reader domain to the methylated histone tail and to both gyres of nucleosomal DNA, explaining the known cooperative interactions. The observed cross-gyre binding may contribute to nucleosome integrity during transcription. The structure also explains how human PWWP domain-containing proteins are recruited to H3K36-methylated regions of the genome for transcription, histone acetylation and methylation, and for DNA methylation and repair.

PubMed: 31819277
DOI: 10.1038/s41594-019-0345-4

実験手法

ELECTRON MICROSCOPY (3.2 Å)