2RSN

Solution structure of the chromodomain of Chp1 in complex with H3K9me3 peptide

2RSN の概要

• エントリーDOI: 10.2210/pdb2rsn/pdb
• 関連するPDBエントリー: 2RSO
• NMR情報: BMRB: 11496
• 分子名称: Chromo domain-containing protein 1, peptide from Histone H3 (2 entities in total)
• 機能のキーワード: chromodomain, protein-peptide complex, rna-mediated gene silencing, chromosomal protein, methylation, nuclear protein
• 由来する生物種: Schizosaccharomyces pombe (Fission yeast); 詳細
• 細胞内の位置: Nucleus: Q10103
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 10935.27

構造登録者

Shimojo, H.,Nishimura, Y. (登録日: 2012-04-18, 公開日: 2012-08-29, 最終更新日: 2025-03-26)

主引用文献

Ishida, M.,Shimojo, H.,Hayashi, A.,Kawaguchi, R.,Ohtani, Y.,Uegaki, K.,Nishimura, Y.,Nakayama, J.
Intrinsic nucleic Acid-binding activity of chp1 chromodomain is required for heterochromatic gene silencing
Mol.Cell, 47:228-241, 2012

PubMed Abstract: Centromeric heterochromatin assembly in fission yeast requires the RNAi pathway. Chp1, a chromodomain (CD) protein, forms the Ago1-containing RNA-induced transcriptional silencing (RITS) complex and recruits siRNA-bound RITS to methylated histone H3 lysine 9 (H3K9me) via its CD. Here, we show that the CD of Chp1 (Chp1-CD) possesses unique nucleic acid-binding activities that are essential for heterochromatic gene silencing. Detailed electrophoretic-mobility shift analyses demonstrated that Chp1 binds to RNA via the CD in addition to its central RNA-recognition motif. Interestingly, robust RNA- and DNA-binding activity of Chp1-CD was strongly enhanced when it was bound to H3K9me, which was revealed to involve a positively charged domain within the Chp1-CD by structural analyses. These results demonstrate a role for the CD that provides a link between RNA, DNA, and methylated histone tails to ensure heterochromatic gene silencing.

PubMed: 22727667
DOI: 10.1016/j.molcel.2012.05.017

実験手法

SOLUTION NMR