8DEI

Structure of the Cac1 KER domain

8DEI の概要

• エントリーDOI: 10.2210/pdb8dei/pdb
• 分子名称: Maltodextrin-binding protein,Chromatin assembly factor 1 subunit p90 fusion, DI(HYDROXYETHYL)ETHER, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: chromatin, dna binding, dna binding protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223150.35

構造登録者

Rosas, R.,Churchill, M.E.A. (登録日: 2022-06-20, 公開日: 2023-07-05, 最終更新日: 2024-02-14)

主引用文献

Rosas, R.,Aguilar, R.R.,Arslanovic, N.,Seck, A.,Smith, D.J.,Tyler, J.K.,Churchill, M.E.A.
A novel single alpha-helix DNA-binding domain in CAF-1 promotes gene silencing and DNA damage survival through tetrasome-length DNA selectivity and spacer function.
Elife, 12:-, 2023

PubMed Abstract: The histone chaperone chromatin assembly factor 1 (CAF-1) deposits two nascent histone H3/H4 dimers onto newly replicated DNA forming the central core of the nucleosome known as the tetrasome. How CAF-1 ensures there is sufficient space for the assembly of tetrasomes remains unknown. Structural and biophysical characterization of the lysine/glutamic acid/arginine-rich (KER) region of CAF-1 revealed a 128-Å single alpha-helix (SAH) motif with unprecedented DNA-binding properties. Distinct KER sequence features and length of the SAH drive the selectivity of CAF-1 for tetrasome-length DNA and facilitate function in budding yeast. In vivo, the KER cooperates with the DNA-binding winged helix domain in CAF-1 to overcome DNA damage sensitivity and maintain silencing of gene expression. We propose that the KER SAH links functional domains within CAF-1 with structural precision, acting as a DNA-binding spacer element during chromatin assembly.

PubMed: 37432722
DOI: 10.7554/eLife.83538

実験手法

X-RAY DIFFRACTION (2.81 Å)