Zabel U, Doye V, Tekotte H, Wepf R, Grandi P, Hurt E C
University of Würzburg, Institut für Pharmakologie und Toxikologie, Germany.
J Cell Biol. 1996 Jun;133(6):1141-52. doi: 10.1083/jcb.133.6.1141.
The amino-terminal domain of Nic96p physically interacts with the Nsp1p complex which is involved in nucleocytoplasmic transport. Here we show that thermosensitive mutations mapping in the central domain of Nic96p inhibit nuclear pore formation at the nonpermissive temperature. Furthermore, the carboxyterminal domain of Nic96p functionally interacts with a novel nucleoporin Nup188p in an allele-specific fashion, and when ProtA-Nup188p was affinity purified, a fraction of Nic96p was found in physical interaction. Although NUP188 is not essential for viability, a null mutant exhibits striking abnormalities in nuclear envelope and nuclear pore morphology. We propose that Nic96p is a multivalent protein of the nuclear pore complex linked to several nuclear pore proteins via its different domains.
Nic96p的氨基末端结构域与参与核质运输的Nsp1p复合物发生物理相互作用。我们在此表明，位于Nic96p中央结构域的温度敏感突变在非允许温度下会抑制核孔形成。此外，Nic96p的羧基末端结构域以等位基因特异性方式与一种新的核孔蛋白Nup188p发生功能相互作用，当对ProtA-Nup188p进行亲和纯化时，发现一部分Nic96p存在物理相互作用。虽然NUP188对细胞活力并非必需，但一个缺失突变体在核膜和核孔形态上表现出显著异常。我们提出，Nic96p是核孔复合体的一种多价蛋白，通过其不同结构域与几种核孔蛋白相连。
