THE PEPTIDE REPEAT DOMAIN OF NUCLEOPORIN NUP98 FUNCTIONS AS A DOCKING SITE IN TRANSPORT ACROSS THE NUCLEAR-PORE COMPLEX
THE PEPTIDE REPEAT DOMAIN OF NUCLEOPORIN NUP98 FUNCTIONS AS A DOCKING SITE IN TRANSPORT ACROSS THE NUCLEAR-PORE COMPLEX
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DOI：
10.1016/0092-8674(95)90331-3
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发表时间：
1995-04-21
期刊：
影响因子：
64.5
通讯作者：
BLOBEL, G
中科院分区：
文献类型：
--
作者：
RADU, A;MOORE, MS;BLOBEL, G
本文报道了大鼠麦胚凝集素反应性核孔复合物（NPC）蛋白的cDNA推导的一级结构。该蛋白质称为Nup 98（98 kDa的核孔蛋白），含有大量的GFG和FG重复序列以及一些FXFG重复序列，因此是先前在酵母中发现的GFG核孔蛋白家族的脊椎动物成员。免疫电镜显示Nup 98不对称地位于NPC的核质侧。Nup 98在模型转运底物的胞质对接活性介导的结合中作为几个对接位点核孔蛋白之一发挥作用。Nup 98的对接位点被映射到其N-末端的一半，其包含所有的肽重复序列。该区域的重组片段耗尽了胞质溶胶的对接活性。我们认为，Nup 98的肽重复结构域，与其他核孔蛋白的肽重复结构域，形成一个阵列的网站介导的对接运输基板，并通过重复的对接和undocking反应的NPC的双向运输收益。
We report the cDNA deduced primary structure of a wheat germ agglutinin-reactive nuclear pore complex (NPC) protein of rat. The protein, termed Nup98 (for nucleoporin of 98 kDa), contains numerous GLFG and FG repeats and some FXFG repeats and is thus a vertebrate member of a family of GLFG nucleoporins that were previously discovered in yeast. Immunoelectron microscopy showed Nup98 to be asymmetrically located at the nucleoplasmic side of the NPC. Nup98 functions as one of several docking site nucleoporins in a cytosolic docking activity-mediated binding of a model transport substrate. The docking site of Nup98 was mapped to its N-terminal half, which contains all of the peptide repeats. A recombinant segment of this region depleted the docking activity of cytosol. We suggest that the peptide repeat domain of Nup98, together with peptide repeat domains of other nucleoporins, forms an array of sites for mediated docking of transport substrate, and that bidirectional transport across the NPC proceeds by repeated docking and undocking reactions.