5EJO

Crystal structure of the winged helix domain in Chromatin assembly factor 1 subunit p90

5EJO の概要

• エントリーDOI: 10.2210/pdb5ejo/pdb
• 分子名称: Chromatin assembly factor 1 subunit p90 (2 entities in total)
• 機能のキーワード: chromatin assembly factor 1, winged helix domain, nucleosome assembly, nuclear protein
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• 細胞内の位置: Nucleus: Q12495
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10549.08

構造登録者

Zhang, K.,Gao, Y.,Li, J.,Burgess, R.,Han, J.,Liang, H.,Zhang, Z.,Liu, Y. (登録日: 2015-11-02, 公開日: 2016-03-16, 最終更新日: 2024-03-20)

主引用文献

Zhang, K.,Gao, Y.,Li, J.,Burgess, R.,Han, J.,Liang, H.,Zhang, Z.,Liu, Y.
A DNA binding winged helix domain in CAF-1 functions with PCNA to stabilize CAF-1 at replication forks
Nucleic Acids Res., 44:5083-5094, 2016

PubMed Abstract: Chromatin assembly factor 1 (CAF-1) is a histone H3-H4 chaperone that deposits newly synthesized histone (H3-H4)2 tetramers during replication-coupled nucleosome assembly. However, how CAF-1 functions in this process is not yet well understood. Here, we report the crystal structure of C terminus of Cac1 (Cac1C), a subunit of yeast CAF-1, and the function of this domain in stabilizing CAF-1 at replication forks. We show that Cac1C forms a winged helix domain (WHD) and binds DNA in a sequence-independent manner. Mutations in Cac1C that abolish DNA binding result in defects in transcriptional silencing and increased sensitivity to DNA damaging agents, and these defects are exacerbated when combined with Cac1 mutations deficient in PCNA binding. Similar phenotypes are observed for corresponding mutations in mouse CAF-1. These results reveal a mechanism conserved in eukaryotic cells whereby the ability of CAF-1 to bind DNA is important for its association with the DNA replication forks and subsequent nucleosome assembly.

PubMed: 26908650
DOI: 10.1093/nar/gkw106

実験手法

X-RAY DIFFRACTION (2.75 Å)