Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones
Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones
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酵母组蛋白伴侣 Hif1 的结构见解：一种将蛋白复合物招募到核心组蛋白的支架蛋白。
DOI：
10.1042/bj20131640
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发表时间：
2014-09-15
影响因子：
4.1
通讯作者：
Niu, Liwen
中科院分区：
文献类型：
--
作者：
Liu, Hejun;Zhang, Mengying;Niu, Liwen
酵母 Hif1 [Hat1（组蛋白乙酰转移酶 1）相互作用因子] 是人类 NASP（核自身抗原精子蛋白）的同源物，是一种组蛋白伴侣，参与各种蛋白复合物，在端粒沉默和染色质重组过程中修饰组蛋白。为了阐明Hif1的结构基础，在本文中，我们展示了Hif1的晶体结构，该结构由超螺旋TPR（四肽重复）结构域和覆盖TPR结构域后部的延伸酸环组成，这代表了SHNi-TPR [Sim3（起始独立于有丝分裂3）-Hif1-NASP中断的TPR]蛋白的典型特征。我们的结合测定表明 Hif1 可以通过组蛋白 H3 和 H4 与组蛋白八聚体结合。酸环被证明对于组蛋白的结合至关重要，并且还可能改变 TPR 沟的构象。通过与核心组蛋白复合物结合，Hif1 可以招募功能性蛋白复合物，在染色质重组过程中修饰组蛋白。
Yeast Hif1 [Hat1 (histone acetyltransferase 1)-interacting factor], a homologue of human NASP (nuclear autoantigenic sperm protein), is a histone chaperone that is involved in various protein complexes which modify histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, in the present paper we demonstrate the crystal structure of Hif1 consisting of a superhelixed TPR (tetratricopeptide repeat) domain and an extended acid loop covering the rear of TPR domain, which represent typical characteristics of SHNi-TPR [Sim3 (start independent of mitosis 3)-Hif1-NASP interrupted TPR] proteins. Our binding assay indicates that Hif1 could bind to the histone octamer via histones H3 and H4. The acid loop is shown to be crucial for the binding of histones and may also change the conformation of the TPR groove. By binding to the core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.