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 Ndclp localization colocalize with a known SPB component, Spc42p. Immunoelectron microscopy shows that Ndclp 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 Ndclp is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1789-1800 |
| Number of pages | 12 |
| Journal | Journal of Cell Biology |
| Volume | 143 |
| Issue number | 7 |
| DOIs | |
| State | Published - Dec 28 1998 |
| Externally published | Yes |
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Keywords
- Ndc1p
- Nuclear pore complex
- Pom152p
- Spindle pole body
- Yeast
ASJC Scopus subject areas
- Cell Biology
Cite this
Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. / Chial, Heidi J.; Rout, Michael P.; Giddings, Thomas H.; Winey, Mark.
In: Journal of Cell Biology, Vol. 143, No. 7, 28.12.1998, p. 1789-1800.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies
AU - Chial, Heidi J.
AU - Rout, Michael P.
AU - Giddings, Thomas H.
AU - Winey, Mark
PY - 1998/12/28
Y1 - 1998/12/28
N2 - 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 Ndclp localization colocalize with a known SPB component, Spc42p. Immunoelectron microscopy shows that Ndclp 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 Ndclp is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE.
AB - 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 Ndclp localization colocalize with a known SPB component, Spc42p. Immunoelectron microscopy shows that Ndclp 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 Ndclp is a shared component of NPCs and SPBs and propose a shared function in the assembly of these organelles into the NE.
KW - Ndc1p
KW - Nuclear pore complex
KW - Pom152p
KW - Spindle pole body
KW - Yeast
UR - http://www.scopus.com/inward/record.url?scp=0032576588&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0032576588&partnerID=8YFLogxK
U2 - 10.1083/jcb.143.7.1789
DO - 10.1083/jcb.143.7.1789
M3 - Article
C2 - 9864355
AN - SCOPUS:0032576588
VL - 143
SP - 1789
EP - 1800
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 7
ER -