Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies.

Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies.
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DOI:
10.1083/jcb.143.7.1789
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发表时间:
1998-12-28
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Winey M
Winey M
中科院分区:
其他
文献类型:
--
作者:
Chial HJ;Rout MP;Giddings TH;Winey M

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我们报告了我们对酿酒酵母 NDC1 基因的研究揭示了核孔复合体 (NPC) 和纺锤体极体 (SPB) 之间的新联系。尽管 NPC 和 SPB 均嵌入酵母的核膜 (NE) 中,但它们的已知功能却截然不同。先前的工作表明,NDC1 功能是正确的 SPB 复制所必需的(Winey, M., M.A. Hoyt, C. Chan, L. Goetsch, D. Botstein, and B. Byers. 1993. J. Cell Biol. 122:743–751)。在这里,我们证明 Ndc1p 是 NE 的膜蛋白,定位于 NPC 和 SPB。间接免疫荧光显微镜显示,Ndc1p 显示出点状核外周定位,与已知的 NPC 成分 Nup49p 共定位。此外,Ndc1p 定位的不同点与已知的 SPB 组件 Spc42p 共定位。免疫电镜显示 Ndc1p 定位于 NPC 和 SPB 与 NE 相互作用的区域。 ndc1-1 突变细胞中的 NPC 在不允许的温度下似乎能正常发挥作用。最后,我们发现 POM152(编码丰富但非必需的核孔蛋白)的缺失可以抑制与 NDC1 基因突变相关的 SPB 重复缺陷。我们证明 Ndc1p 是 NPC 和 SPB 的共享组件,并提出将这些细胞器组装到 NE 中的共享功能。
We report a novel connection between nuclear pore complexes (NPCs) and spindle pole bodies (SPBs) revealed by our studies of the Saccharomyces cerevisiae NDC1 gene. Although both NPCs and SPBs are embedded in the nuclear envelope (NE) in yeast, their known functions are quite distinct. Previous work demonstrated that NDC1 function is required for proper SPB duplication (Winey, M., M.A. Hoyt, C. Chan, L. Goetsch, D. Botstein, and B. Byers. 1993. J. Cell Biol. 122:743–751). Here, we show that Ndc1p is a membrane protein of the NE that localizes to both NPCs and SPBs. Indirect immunofluorescence microscopy shows that Ndc1p displays punctate, nuclear peripheral localization that colocalizes with a known NPC component, Nup49p. Additionally, distinct spots of Ndc1p localization colocalize with a known SPB component, Spc42p. Immunoelectron microscopy shows that Ndc1p localizes to the regions of NPCs and SPBs that interact with the NE. The NPCs in ndc1-1 mutant cells appear to function normally at the nonpermissive temperature. Finally, we have found that a deletion of POM152, which encodes an abundant but nonessential nucleoporin, suppresses the SPB duplication defect associated with a mutation in the NDC1 gene. We show that Ndc1p is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE.