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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex
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Structural and functional analysis of an essential nucleoporin heterotrimer on the cytoplasmic face of the nuclear pore complex

机译：核孔复合物胞质表面上必不可少的核孔蛋白异三聚体的结构和功能分析

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摘要

So far, only a few of the interactions between the ≈30 nucleoporins comprising the modular structure of the nuclear pore complex have been defined at atomic resolution. Here we report the crystal struc ture, at 2.6 A resolution, of a heterotrimeric complex, composed of fragments of three cytoplasmically oriented nucleoporins of yeast: Nup82, Nup116, and Nup159. Our data show that the Nup82 frag ment, representing more than the N-terminal half of the molecule, folds into an extensively decorated, seven-bladed β-propeller that forms the centerpiece of this heterotrimeric complex and anchors both a C-terminal fragment of Nup116 and the C-terminal tail of Nup159. Binding between Nup116 and Nup82 is mutually rein forced via two loops, one emanating from the Nup82 β-propeller and the other one from the β-sandwich fold of Nup116, each con tacting binding pockets in their counterparts. The Nup82-Nup159 interaction occurs through an amphipathic α-helix of Nup159, which is cradled in a large hydrophobic groove that is generated from several large surface decorations of the Nup82 β-propeller. Although Nup159 and Nup116 fragments bind to the Nup82 β-pro peller in close vicinity, there are no direct contacts between them, consistent with the noncooperative binding that was detected bio chemically. Extensive mutagenesis delineated hot-spot residues for these interactions. We also showed that the Nup82 β-propeller binds to other yeast Nup116 family members, Nup145N, Nup100 and to the mammalian homolog, Nup98. Notably, each of the three nucleoporins contains additional nuclear pore complex binding sites, distinct from those that were defined here in the heterotri meric Nup82·Nup159·Nup116 complex.
机译：到目前为止，在原子分辨率上，仅定义了约30个构成核孔复合体模块结构的核孔蛋白之间的相互作用。在这里，我们报道了异三聚体复合物的晶体结构，其分辨率为2.6 A，该复合物由三种胞质定向的酵母核孔蛋白Nup82，Nup116和Nup159的片段组成。我们的数据显示，代表分子N端以上一半的Nup82片段折叠成装饰广泛的七叶β螺旋桨，该螺旋桨形成了此异三聚体复合物的核心，并锚定了C的C端片段Nup116和Nup159的C末端尾巴。 Nup116和Nup82之间的结合是通过两个环相互加强的，一个环来自Nup82β螺旋桨，另一个环来自Nup116的β夹心折叠，每个环在它们的对应物中与结合口袋接触。 Nup82-Nup159相互作用是通过Nup159的两亲性α-螺旋发生的，该螺旋缠绕在一个较大的疏水槽中，该疏水槽由Nup82β螺旋桨的多个大型表面装饰产生。尽管Nup159和Nup116片段与Nup82β-pro螺旋桨紧密结合，但它们之间没有直接接触，这与生物化学检测到的非合作结合是一致的。广泛的诱变描述了这些相互作用的热点残基。我们还显示，Nup82β螺旋桨与其他酵母Nup116家族成员Nup145N，Nup100以及哺乳动物同源物Nup98结合。值得注意的是，三个核孔蛋白中的每一个都包含额外的核孔复合物结合位点，这与杂三聚体Nup82·Nup159·Nup116复合物中此处定义的位点不同。

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