+検索条件
-Structure paper
タイトル | Structure of H3K36-methylated nucleosome-PWWP complex reveals multivalent cross-gyre binding. |
---|---|
ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 27, Issue 1, Page 8-13, Year 2020 |
掲載日 | 2019年12月9日 |
著者 | Haibo Wang / Lucas Farnung / Christian Dienemann / Patrick Cramer / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Struct Mol Biol / PubMed:31819277 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.2 Å |
構造データ | EMDB-10069, PDB-6s01: |
由来 |
|
キーワード | TRANSCRIPTION / LEDGF / PWWP / H3K36me3 / nucleosome |