Siniossoglou S, Wimmer C, Rieger M, Doye V, Tekotte H, Weise C, Emig S, Segref A, Hurt E C
European Molecular Biology Laboratory, Heidelberg Federal Republic of Germany.
Cell. 1996 Jan 26;84(2):265-75. doi: 10.1016/s0092-8674(00)80981-2.
In a genetic screen for nucleoporin-interacting components, a novel nuclear pore protein Nup84p, which exhibits homology to mammalian Nup107p, was isolated. Nup84p forms a complex with five proteins, of which Nup120p, Nup85p, Sec13p, and a Sec13p homolog were identified. Upon isolation of Sec13p-ProtA, nucleoporins were still associated, but the major copurifying band was a 150 kDa protein, showing that Sec13p occurs in two complexes. Disruption of any of the genes encoding Nup84p, Nup85p, or Nup120p caused defects in nuclear membrane and nuclear pore complex organization, as well as in poly(A)+ RNA transport. Thus, the Nup84p complex in conjunction with Sec13-type proteins is required for correct nuclear pore biogenesis.
在一项针对核孔蛋白相互作用成分的遗传筛选中,分离出了一种与哺乳动物Nup107p具有同源性的新型核孔蛋白Nup84p。Nup84p与五种蛋白质形成复合物,其中已鉴定出Nup120p、Nup85p、Sec13p和一种Sec13p同源物。分离出Sec13p-ProtA后,核孔蛋白仍相互关联,但主要的共纯化条带是一种150 kDa的蛋白质,表明Sec13p存在于两种复合物中。编码Nup84p、Nup85p或Nup120p的任何基因的破坏都会导致核膜和核孔复合体组织以及聚腺苷酸(poly(A)+)RNA转运方面的缺陷。因此,Nup84p复合物与Sec13型蛋白共同作用是正确的核孔生物发生所必需的。