7V6Q

Crystal structure of sNASP-ASF1A-H3.1-H4 complex

7V6Q の概要

• エントリーDOI: 10.2210/pdb7v6q/pdb
• 関連するPDBエントリー: 7V6P
• 分子名称: Histone chaperone ASF1A, Histone H3.1, Histone H4, ... (7 entities in total)
• 機能のキーワード: histone chaperone, chaperone
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 153967.69

構造登録者

Liu, C.P.,Xu, R.M. (登録日: 2021-08-20, 公開日: 2021-12-29, 最終更新日: 2023-11-29)

主引用文献

Liu, C.P.,Jin, W.,Hu, J.,Wang, M.,Chen, J.,Li, G.,Xu, R.M.
Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones.
Genes Dev., 35:1610-1624, 2021

PubMed Abstract: Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3-H4 chaperones found in distinct and common complexes, yet how sNASP binds H3-H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3-H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3-H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones.

PubMed: 34819355
DOI: 10.1101/gad.349100.121

実験手法

X-RAY DIFFRACTION (3 Å)