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J. Cell Biol.,
Volume 143, Number 7, December 28, 1998 1789-1800
* Department of Molecular, Cellular, and Developmental Biology, University of Colorado-Boulder, Boulder, Colorado
80309-0347; and 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.
The Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York
10021-6399
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