title: Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies.
abstract: 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.
authors.affiliation: Department of Molecular, Cellular, and Developmental Biology, University of Colorado-Boulder, Boulder, Colorado 80309-0347, USA.
authors.forename: H J
authors.initials: HJ
authors.lastname: Chial
authors.forename: M P
authors.initials: MP
authors.lastname: Rout
authors.forename: T H
authors.initials: TH
authors.lastname: Giddings
authors.forename: M
authors.initials: M
authors.lastname: Winey
mesh_terms: D018385:Centrosome / Q000378:metabolism / Q000648:ultrastructure*; D019084:Fluorescent Antibody Technique, Indirect; D005656:Fungal Proteins / Q000378:metabolism*; D017353:Gene Deletion; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins / Q000172:deficiency / Q000235:genetics / Q000502:physiology; D008565:Membrane Proteins / Q000378:metabolism*; D016253:Microscopy, Immunoelectron; D009685:Nuclear Envelope / Q000378:metabolism / Q000648:ultrastructure*; D022022:Nuclear Pore; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins / Q000172:deficiency / Q000235:genetics / Q000378:metabolism* / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*; D029701:Saccharomyces cerevisiae Proteins
chemical_list: D005656:Fungal Proteins; D046911:Macromolecular Substances; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; C082594:NDC1 protein, S cerevisiae; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; C086449:POM152 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins