A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
A novel nuclear pore protein Nup82p which specifically binds to a fraction of Nsp1p.
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DOI：
10.1083/jcb.130.6.1263
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发表时间：
1995-09
期刊：
影响因子：
--
通讯作者：
Hurt EC
中科院分区：
文献类型：
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作者：
Grandi P;Emig S;Weise C;Hucho F;Pohl T;Hurt EC
Nsp1p与核孔蛋白Nup49p、Nup57p和Nic96p相互作用，形成稳定的复合物，参与核胞质运输。另外一个p80成分与Nsp1p相关，但不与标记的Nup57p、Nup49p和Nic96p共纯化。p80基因被克隆并编码一种新的必需核孔蛋白Nup82p。标记的Nup82p的免疫沉淀显示，它与Nsp1p的一部分物理相关，这与Nup57p， Nic96p和Nup49p复合物中的Nsp1p不同。Nup82蛋白可以分为至少两个不同的结构域，这两个结构域都是必需的基本功能，但它只是羧基末端结构域，表现出七磷酸重复，与Nsp1p结合。缺失nsp82p的酵母细胞会停止细胞生长，并同时显示poly(a)+RNA输出缺陷，但EM未观察到核膜结构和核孔密度的重大改变。这表明Nsp1p参与了NPC的多种相互作用，因此具有与不同NPC结构物理相互作用的能力。
Nsp1p interacts with nuclear pore proteins Nup49p, Nup57p and Nic96p in a stable complex which participates in nucleocytoplasmic transport. An additional p80 component is associated with Nsp1p, but does not co- purify with tagged Nup57p, Nup49p and Nic96p. The p80 gene was cloned and encodes a novel essential nuclear pore protein named Nup82p. Immunoprecipitation of tagged Nup82p reveals that it is physically associated with a fraction of Nsp1p which is distinct from Nsp1p found in a complex with Nup57p, Nic96p and Nup49p. The Nup82 protein can be divided into at least two different domains both required for the essential function, but it is only the carboxy-terminal domain, exhibiting heptad repeats, which binds to Nsp1p. Yeast cells depleted of Nup82p stop cell growth and concomitantly show a defect in poly(A)+RNA export, but no major alterations of nuclear envelope structure and nuclear pore density are seen by EM. This shows that Nsp1p participates in multiple interactions at the NPC and thus has the capability to physically interact with different NPC structures.