Hif1蛋白结合组蛋白H2A-H2B二聚体和H3-H4四聚体的结构生物学研究  

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

作　　者：Mengying Zhang 刘合军 Yongxiang Gao Zhongliang Zhu Zijun Chen Peiyi Zheng Lu Xue Jixi Li 滕脉坤[2] 牛立文[2] 

机构地区：[1]不详 [2]中国科学技术大学生命科学学院

出　　处：《科学新闻》2017年第4期183-183,共1页Science News

基　　金：科技部973项目(2012CB917200、2011CBA00800);国家自然科学基金项目(31130018、31170726)的共同经费资助

摘　　要：组蛋白分子伴侣通过严格调控组蛋白的翻译后修饰，确保了核小体组装及解聚过程中组蛋白的正确沉积及解离，进而调节染色质结构并改变基因活性。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.

关 键 词：蛋白 结构 生物学 分子伴侣 染色质 基因 

分 类 号：Q510.3[生物学—生物化学]