5BT1

histone chaperone Hif1 playing with histone H2A-H2B dimer

5BT1 の概要

• エントリーDOI: 10.2210/pdb5bt1/pdb
• 関連するPDBエントリー: 4NQ0
• 分子名称: HAT1-interacting factor 1, Histone H2A.1, Histone H2B.1, ... (4 entities in total)
• 機能のキーワード: histone chaperone complex, tpr, nasp homolog, assembly, chaperone
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• 細胞内の位置: Nucleus : Q12373 P04911 P02293
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 119998.74

構造登録者

Liu, H.,Zhang, M.,Gao, Y.,Teng, M.,Niu, L. (登録日: 2015-06-02, 公開日: 2016-10-26, 最終更新日: 2023-11-08)

主引用文献

Zhang, M.,Liu, H.,Gao, Y.,Zhu, Z.,Chen, Z.,Zheng, P.,Xue, L.,Li, J.,Teng, M.,Niu, L.
Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer
Structure, 24:1810-1820, 2016

PubMed Abstract: Histone chaperones are critical for guiding specific post-transcriptional modifications of histones, safeguarding the histone deposition (or disassociation) of nucleosome (dis)assembly, and regulating chromatin structures to change gene activities. HAT1-interacting factor 1 (Hif1) has been reported to be an H3-H4 chaperone and to be involved in telomeric silencing and nucleosome (dis)assembly. However, the structural basis for the interaction of Hif1 with histones remains unknown. Here, we report the complex structure of Hif1 binding to H2A-H2B for uncovering the chaperone specificities of Hif1 on binding to both the H2A-H2B dimer and the H3-H4 tetramer. Our findings reveal that Hif1 interacts with the H2A-H2B dimer and the H3-H4 tetramer via distinct mechanisms, suggesting that Hif1 is a pivotal scaffold on alternate binding of H2A-H2B and H3-H4. These specificities are conserved features of the Sim3-Hif1-NASP interrupted tetratricopeptide repeat proteins, which provide clues for investigating their potential roles in nucleosome (dis)assembly.

PubMed: 27618665
DOI: 10.1016/j.str.2016.08.001

実験手法

X-RAY DIFFRACTION (2.62 Å)