The Crystal Structure of the Human Nascent Polypeptide-Associated Complex Domain Reveals a Nucleic Acid-Binding Region on the NACA Subunit
The Crystal Structure of the Human Nascent Polypeptide-Associated Complex Domain Reveals a Nucleic Acid-Binding Region on the NACA Subunit
复制标题
人类新生多肽相关复合结构域的晶体结构揭示了 NACA 亚基上的核酸结合区域
DOI：
10.1021/bi902050p
复制
发表时间：
2010-04-06
期刊：
影响因子：
2.9
通讯作者：
Teng, Maikun
中科院分区：
文献类型：
--
作者：
Liu, Yiwei;Hu, Yingxia;Teng, Maikun
在古细菌和真核生物中，新生多肽相关复合物（NAC）是胞质分子伴侣之一，其在新生多肽链从核糖体出现时接触新生多肽链并协助翻译后过程。真核生物NAC是异源二聚体，其两个亚基通过称为NAC结构域的二聚化结构域形成稳定的复合物。除了作为蛋白质翻译伴侣外，NAC亚基还在转录调控中单独发挥作用。在这里，我们报告的晶体结构的人NAC域，揭示了人类NAC二聚化的方式。基于该结构，我们鉴定了人NAC α-亚基的NAC结构域中的一个区域作为新的核酸结合区域，该区域被β-亚基中的螺旋区域阻断而不能结合异二聚体复合物中的核酸。
In archaea and eukaryotes, the nascent polypeptide-associated complex (NAC) is one of the cytosolic chaperones that contact the nascent polypeptide chains as they emerge from the ribosome and assist in post-translational processes. The eukaryotic NAC is a heterodimer, and its two subunits form a stable complex through a dimerizing domain called the NAC domain. In addition to acting as a protein translation chaperone, the NAC subunits also function individually in transcriptional regulation. Here we report the crystal structure of the human NAC domain, which reveals the manner of human NAC dimerization. On the basis of the structure, we identified a region in the NAC domain of the human NAC alpha-subunit as a new nucleic acid-binding region, which is blocked from binding nucleic acids in the heterodimeric complex by a helix region in the beta-subunit.