Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer

被引:15
作者
Zhang, Mengying [1 ,2 ,3 ]
Liu, Hejun [1 ,2 ,3 ]
Gao, Yongxiang [1 ,2 ,3 ]
Zhu, Zhongliang [1 ,2 ,3 ]
Chen, Zijun [4 ,5 ]
Zheng, Peiyi [1 ,2 ,3 ]
Xue, Lu [1 ,2 ,3 ]
Li, Jixi [4 ,5 ]
Teng, Maikun [1 ,2 ,3 ]
Niu, Liwen [1 ,2 ,3 ]
机构
[1] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, Hefei 230026, Anhui, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China
[3] Chinese Acad Sci, Key Lab Struct Biol, Hefei 230026, Anhui, Peoples R China
[4] Fudan Univ, State Key Lab Genet Engn, Shanghai 200438, Peoples R China
[5] Fudan Univ, Sch Life Sci, Shanghai 200438, Peoples R China
基金
中国国家自然科学基金;
关键词
ACETYLTRANSFERASE-B; CHAPERONE; CHROMATIN; DNA; COMPLEX; NASP; TRANSCRIPTION; SPECIFICITY; PROTEIN; EXCHANGE;
D O I
10.1016/j.str.2016.08.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1810 / 1820
页数:11
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