메뉴 건너뛰기




Volumn 3, Issue 2, 2004, Pages 447-458

A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndc1p in nuclear pore assembly

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; NDC1 PROTEIN, S CEREVISIAE; NIC96 PROTEIN, S CEREVISIAE; NUCLEAR PROTEIN; NUCLEOPORIN; NUP49 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 8444225640     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.3.2.447-458.2004     Document Type: Article
Times cited : (49)

References (45)
  • 1
    • 0034255733 scopus 로고    scopus 로고
    • Spindle pole body duplication: A model for centrosome duplication?
    • Adams, I. R., and J. V. Kilmartin. 2000. Spindle pole body duplication: a model for centrosome duplication? Trends Cell Biol. 10:329-335.
    • (2000) Trends Cell Biol. , vol.10 , pp. 329-335
    • Adams, I.R.1    Kilmartin, J.V.2
  • 2
    • 0031019245 scopus 로고    scopus 로고
    • Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells
    • Belgareh, N., and V. Doye. 1997. Dynamics of nuclear pore distribution in nucleoporin mutant yeast cells. J. Cell Biol. 136:747-759.
    • (1997) J. Cell Biol. , vol.136 , pp. 747-759
    • Belgareh, N.1    Doye, V.2
  • 3
    • 0032841066 scopus 로고    scopus 로고
    • Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis
    • Bodoor, K., S. Shaikh, D. Salina, W. H. Raharjo, R. Bastos, M. Lohka, and B. Burke. 1999. Sequential recruitment of NPC proteins to the nuclear periphery at the end of mitosis. J. Cell Sci. 112:2253-2264.
    • (1999) J. Cell Sci. , vol.112 , pp. 2253-2264
    • Bodoor, K.1    Shaikh, S.2    Salina, D.3    Raharjo, W.H.4    Bastos, R.5    Lohka, M.6    Burke, B.7
  • 4
    • 0023484186 scopus 로고
    • 5-Fluoroorotic acid as a selective agent in yeast molecular genetics
    • Boeke, J. D., J. Trueheart, G. Natsoulis, and G. R. Fink. 1987. 5-Fluoroorotic acid as a selective agent in yeast molecular genetics. Methods Enzymol. 154:164-175.
    • (1987) Methods Enzymol. , vol.154 , pp. 164-175
    • Boeke, J.D.1    Trueheart, J.2    Natsoulis, G.3    Fink, G.R.4
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C. B., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14:115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 0030793799 scopus 로고    scopus 로고
    • In vivo dynamics of nuclear pore complexes in yeast
    • Bucci, M., and S. R. Wente. 1997. In vivo dynamics of nuclear pore complexes in yeast. J. Cell Biol. 136:1185-1199.
    • (1997) J. Cell Biol. , vol.136 , pp. 1185-1199
    • Bucci, M.1    Wente, S.R.2
  • 7
    • 0031688617 scopus 로고    scopus 로고
    • A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly
    • Bucci, M., and S. R. Wente. 1998. A novel fluorescence-based genetic strategy identifies mutants of Saccharomyces cerevisiae defective for nuclear pore complex assembly. Mol. Biol. Cell 9:2439-2461.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2439-2461
    • Bucci, M.1    Wente, S.R.2
  • 9
    • 0037017394 scopus 로고    scopus 로고
    • The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p
    • Castillo, A. R., J. B. Meehl, G. Morgan, A. Schutz-Geschwender, and M. Winey. 2002. The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p. J. Cell Biol. 156:453-465.
    • (2002) J. Cell Biol. , vol.156 , pp. 453-465
    • Castillo, A.R.1    Meehl, J.B.2    Morgan, G.3    Schutz-Geschwender, A.4    Winey, M.5
  • 10
    • 0033621063 scopus 로고    scopus 로고
    • Altered dosage of the Saccharomyces cerevisiae spindle pole body duplication gene, NDC1, leads to aneuploidy and polyploidy
    • Chial, H. J., T. H. Giddings, Jr., E. A, Siewert, M. A. Hoyt, and M. Winey. 1999. Altered dosage of the Saccharomyces cerevisiae spindle pole body duplication gene, NDC1, leads to aneuploidy and polyploidy. Proc. Natl. Acad. Sci. USA 96:10200-10205.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10200-10205
    • Chial, H.J.1    Giddings Jr., T.H.2    Siewert, E.A.3    Hoyt, M.A.4    Winey, M.5
  • 11
    • 0032576588 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies
    • Chial, H. J., M. P. Rout, T. H. Giddings, Jr., and M. Winey. 1998. Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. J. Cell Biol. 143:1789-1800.
    • (1998) J. Cell Biol. , vol.143 , pp. 1789-1800
    • Chial, H.J.1    Rout, M.P.2    Giddings Jr., T.H.3    Winey, M.4
  • 12
    • 0033304105 scopus 로고    scopus 로고
    • Mechanisms of genetic instability revealed by analysis of yeast spindle pole body duplication
    • Chial, H. J., and M. Winey. 1999. Mechanisms of genetic instability revealed by analysis of yeast spindle pole body duplication. Biol. Cell 91:439-450.
    • (1999) Biol. Cell , vol.91 , pp. 439-450
    • Chial, H.J.1    Winey, M.2
  • 13
    • 0037043334 scopus 로고    scopus 로고
    • Interference with the cytoplasmic tail of gp210 disrupts "close opposition" of nuclear membranes and blocks nuclear pore dilation
    • Drummond, S. P., and K. L. Wilson. 2002. Interference with the cytoplasmic tail of gp210 disrupts "close opposition" of nuclear membranes and blocks nuclear pore dilation. J. Cell Biol. 158:53-62.
    • (2002) J. Cell Biol. , vol.158 , pp. 53-62
    • Drummond, S.P.1    Wilson, K.L.2
  • 14
    • 33846074019 scopus 로고    scopus 로고
    • Using rapid freeze and freeze-substitution for the preparation of yeast cells for electron microscopy and three-dimensional analysis
    • Giddings, T. H., Jr., E. T. O'Toole, M. Morphew, D. N. Mastronarde, J. R. McIntosh, and M. Winey. 2001. Using rapid freeze and freeze-substitution for the preparation of yeast cells for electron microscopy and three-dimensional analysis. Methods Cell Biol. 67:27-42.
    • (2001) Methods Cell Biol. , vol.67 , pp. 27-42
    • Giddings Jr., T.H.1    O'Toole, E.T.2    Morphew, M.3    Mastronarde, D.N.4    McIntosh, J.R.5    Winey, M.6
  • 17
    • 0018699773 scopus 로고
    • Microbial determinations by flow cytometry
    • Hutter, K. J., and H. E. Eipel. 1979. Microbial determinations by flow cytometry. J. Gen. Microbiol. 113:369-375.
    • (1979) J. Gen. Microbiol. , vol.113 , pp. 369-375
    • Hutter, K.J.1    Eipel, H.E.2
  • 18
    • 0037164818 scopus 로고    scopus 로고
    • Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p
    • Jaspersen, S. L., T. H. Giddings, Jr., and M. Winey. 2002. Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. J. Cell Biol. 159:945-956.
    • (2002) J. Cell Biol. , vol.159 , pp. 945-956
    • Jaspersen, S.L.1    Giddings Jr., T.H.2    Winey, M.3
  • 19
    • 0141864663 scopus 로고    scopus 로고
    • Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication
    • Kilmartin, J. V. 2003. Sfi1p has conserved centrin-binding sites and an essential function in budding yeast spindle pole body duplication. J. Cell Biol. 162:1211-1221.
    • (2003) J. Cell Biol. , vol.162 , pp. 1211-1221
    • Kilmartin, J.V.1
  • 20
    • 0032775010 scopus 로고    scopus 로고
    • Epitope tagging of yeast genes using a PCR-based strategy: More tags and improved practical routines
    • Knop, M., K. Siegers, G. Pereira, W. Zachariae, B. Winsor, K. Nasmyth, and E. Schiebel. 1999. Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines. Yeast 15:963-972.
    • (1999) Yeast , vol.15 , pp. 963-972
    • Knop, M.1    Siegers, K.2    Pereira, G.3    Zachariae, W.4    Winsor, B.5    Nasmyth, K.6    Schiebel, E.7
  • 21
    • 0029897642 scopus 로고    scopus 로고
    • Dynamic localization of the nuclear import receptor and its interactions with transport factors
    • Koepp, D. M., D. H. Wong, A. H. Corbett, and P. A. Silver. 1996. Dynamic localization of the nuclear import receptor and its interactions with transport factors. J. Cell Biol. 133:1163-1176.
    • (1996) J. Cell Biol. , vol.133 , pp. 1163-1176
    • Koepp, D.M.1    Wong, D.H.2    Corbett, A.H.3    Silver, P.A.4
  • 22
    • 0033529625 scopus 로고    scopus 로고
    • Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane
    • Kosova, B., N. Pante, C. Rollenhagen, and E. Hurt 1999. Nup192p is a conserved nucleoporin with a preferential location at the inner site of the nuclear membrane. J. Biol. Chem. 274:22646-22651.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22646-22651
    • Kosova, B.1    Pante, N.2    Rollenhagen, C.3    Hurt, E.4
  • 23
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A., J. D. Roberts, and R. A. Zakour. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 24
    • 0035858867 scopus 로고    scopus 로고
    • A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope
    • Marelli, M., C. P. Lust, H. Chan, J. D. Aitchison, and R. W. Wozniak. 2001. A link between the synthesis of nucleoporins and the biogenesis of the nuclear envelope. J. Cell Biol. 153:709-723.
    • (2001) J. Cell Biol. , vol.153 , pp. 709-723
    • Marelli, M.1    Lust, C.P.2    Chan, H.3    Aitchison, J.D.4    Wozniak, R.W.5
  • 25
    • 0027053912 scopus 로고
    • NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation
    • Mutvei, A., S. Dihlmann, W. Herth, and E. C. Hurt 1992. NSP1 depletion in yeast affects nuclear pore formation and nuclear accumulation. Eur. J. Cell Biol. 59:280-295.
    • (1992) Eur. J. Cell Biol. , vol.59 , pp. 280-295
    • Mutvei, A.1    Dihlmann, S.2    Herth, W.3    Hurt, E.C.4
  • 26
    • 0033053359 scopus 로고    scopus 로고
    • High-voltage electron tomography of spindle pole bodies and early mitotic spindles in the yeast Saccharomyces cerevisiae
    • O'Toole, E. T., M. Winey, and J. R. McIntosh. 1999. High-voltage electron tomography of spindle pole bodies and early mitotic spindles in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell 10:2017-2031.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2017-2031
    • O'Toole, E.T.1    Winey, M.2    McIntosh, J.R.3
  • 27
    • 0025979877 scopus 로고
    • Targeting, disruption, replacement, and allele rescue: Integrative DNA transformation in yeast
    • Rothstein, R. 1991. Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194:281-301.
    • (1991) Methods Enzymol. , vol.194 , pp. 281-301
    • Rothstein, R.1
  • 28
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M. P., J. D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B. T. Chait 2000. The yeast nuclear pore complex: composition, architecture, and transport mechanism. J. Cell Biol. 148:635-651.
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 29
    • 0344670185 scopus 로고    scopus 로고
    • The Ran GTPase cycle is required for yeast nuclear pore complex assembly
    • Ryan, K. J., J. M. McCaffery, and S. R. Wente. 2003. The Ran GTPase cycle is required for yeast nuclear pore complex assembly. J. Cell Biol. 160:1041-1053.
    • (2003) J. Cell Biol. , vol.160 , pp. 1041-1053
    • Ryan, K.J.1    McCaffery, J.M.2    Wente, S.R.3
  • 30
    • 2942578315 scopus 로고    scopus 로고
    • Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly
    • Ryan, K. J., and S. R. Wente. 2002. Isolation and characterization of new Saccharomyces cerevisiae mutants perturbed in nuclear pore complex assembly. BMC Genet. 3:17.
    • (2002) BMC Genet. , vol.3 , pp. 17
    • Ryan, K.J.1    Wente, S.R.2
  • 32
    • 0034142341 scopus 로고    scopus 로고
    • The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is essential for SPB duplication
    • Schramm, C., S. Elliott, A. Shevchenko, A. Shevchenko, and E. Schiebel. 2000. The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is essential for SPB duplication. EMBO J. 19:421-433.
    • (2000) EMBO J. , vol.19 , pp. 421-433
    • Schramm, C.1    Elliott, S.2    Shevchenko, A.3    Shevchenko, A.4    Schiebel, E.5
  • 33
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and P. Hieter. 1989. A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122:19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 34
    • 0037604556 scopus 로고    scopus 로고
    • Peering through the pore: Nuclear pore complex structure, assembly, and function
    • Suntharalingam, M., and S. R. Wente. 2003. Peering through the pore: nuclear pore complex structure, assembly, and function. Dev. Cell 4:775-789.
    • (2003) Dev. Cell , vol.4 , pp. 775-789
    • Suntharalingam, M.1    Wente, S.R.2
  • 35
    • 0022461695 scopus 로고
    • A gene required for the separation of chromosomes on the spindle apparatus in yeast
    • Thomas, J. H., and D. Botstein. 1986. A gene required for the separation of chromosomes on the spindle apparatus in yeast. Cell 44:65-76.
    • (1986) Cell , vol.44 , pp. 65-76
    • Thomas, J.H.1    Botstein, D.2
  • 36
    • 0035370938 scopus 로고    scopus 로고
    • Nuclear pores and nuclear assembly
    • Vasu, S. K., and D. J. Forbes. 2001. Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13:363-375.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 363-375
    • Vasu, S.K.1    Forbes, D.J.2
  • 37
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., A. Brachat, R. Pohlmann, and P. Philippsen. 1994. New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10:1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 38
    • 0031667188 scopus 로고    scopus 로고
    • +: A gene required for cell cycle-dependent spindle pole body anchoring in the nuclear envelope and bipolar spindle formation in Schizosaccharomyces pombe
    • +: a gene required for cell cycle-dependent spindle pole body anchoring in the nuclear envelope and bipolar spindle formation in Schizosaccharomyces pombe. Mol. Biol. Cell 9:2839-2855.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2839-2855
    • West, R.R.1    Vaisberg, E.V.2    Ding, R.3    Nurse, P.4    McIntosh, J.R.5
  • 39
    • 0025779517 scopus 로고
    • MPS1 and MPS2: Novel yeast genes defining distinct steps of spindle pole body duplication
    • Winey, M., L. Goetsch, P. Baum, and B. Byers. 1991. MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication. J. Cell Biol. 114:745-754.
    • (1991) J. Cell Biol. , vol.114 , pp. 745-754
    • Winey, M.1    Goetsch, L.2    Baum, P.3    Byers, B.4
  • 40
    • 0027237823 scopus 로고
    • NDC1: A nuclear periphery component required for yeast spindle pole body duplication
    • Winey, M., M. A. Hoyt, C. Chan, L. Goetsch, D. Botstein, and B. Byers. 1993. NDC1: a nuclear periphery component required for yeast spindle pole body duplication. J. Cell Biol. 122:743-751.
    • (1993) J. Cell Biol. , vol.122 , pp. 743-751
    • Winey, M.1    Hoyt, M.A.2    Chan, C.3    Goetsch, L.4    Botstein, D.5    Byers, B.6
  • 41
    • 0030776030 scopus 로고    scopus 로고
    • Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes
    • Winey, M., D. Yarar, T. H. Giddings, Jr., and D. N. Mastronarde. 1997. Nuclear pore complex number and distribution throughout the Saccharomyces cerevisiae cell cycle by three-dimensional reconstruction from electron micrographs of nuclear envelopes. Mol. Biol. Cell 8:2119-2132.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2119-2132
    • Winey, M.1    Yarar, D.2    Giddings Jr., T.H.3    Mastronarde, D.N.4
  • 42
    • 0028313943 scopus 로고
    • POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope
    • Wozniak, R. W., G. Blobel, and M. P. Rout 1994. POM152 is an integral protein of the pore membrane domain of the yeast nuclear envelope. J. Cell Biol. 125:31-42.
    • (1994) J. Cell Biol. , vol.125 , pp. 31-42
    • Wozniak, R.W.1    Blobel, G.2    Rout, M.P.3
  • 43
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang, Q., M. P. Rout, and C. W. Akey. 1998. Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1:223-234.
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 44
    • 0029900425 scopus 로고    scopus 로고
    • Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p
    • Zabel, U., V. Doye, H. Tekotte, R. Wepf, P. Grandi, and E. C. Hurt. 1996. Nic96p is required for nuclear pore formation and functionally interacts with a novel nucleoporin, Nup188p. J. Cell Biol. 133:1141-1152.
    • (1996) J. Cell Biol. , vol.133 , pp. 1141-1152
    • Zabel, U.1    Doye, V.2    Tekotte, H.3    Wepf, R.4    Grandi, P.5    Hurt, E.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.