GLE2, a Saccharomyces cerevisiae homologue of the Schizosaccharomyces pombe export factor RAE1, is required for nuclear pore complex structure and function

Molecular Biology of the Cell

Volumn 7, Issue 12, 1996, Pages 1921-1937

  Murphy, Robert ^a   Watkins, Janis L ^a   Wente, Susan R ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; CELL NUCLEUS MEMBRANE; GENE ISOLATION; INTRACELLULAR TRANSPORT; NONHUMAN; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE; SEQUENCE HOMOLOGY;

SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE;

EID: 0029804758     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.7.12.1921     Document Type: Article

References (100)

1. Adam, E.J., and Adam, S.A. (1994). Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope. J. Cell Biol. 125, 547-555.
2. Adam, S.A. (1995). The importance of importin. Trends Cell Biol. 5, 189-191.
3. Aebi, M., Clark, M.W., Vijayraghavan, U., and Abelson, J. (1990). A yeast mutant, PRP20, altered in mRNA metabolism and maintenance of the nuclear structure, is defective in a gene homologous to the human gene RCC1 which is involved in the control of chromosome condensation. Mol. Gen. Genet. 224, 72-80.
4. Aitchison, J.D., Blobel, G., and Rout, M.P. (1995a). Nup120p - a yeast nucleoporin required for NPC distribution and mRNA transport. J. Cell Biol. 131, 1659-1675.
5. Aitchison, J.D., Rout, M.P., Marelli, M., Blobel, G., and Wozniak, R.W. (1995b). Two novel related yeast nucleoporins Nup170p and Nup157p - complementation with the vertebrate homologue Nup155p and functional interactions with the yeast nuclear pore-membrane protein Pom152p. J. Cell Biol. 131, 1133-1148.
6. Amberg, D.C., Fleischmann, M., Stagljar, I., Cole, C.N., and Aebi, M. (1993). Nuclear PRP20 protein is required for mRNA export. EMBO J. 12, 233-241.
7. Amberg, D.C., Goldstein, A.L., and Cole, C.N. (1992). Isolation and characterization of RAT1: an essential gene of Saccharomyces cerevisiae required for the efficient nucleocytoplasmic trafficking of mRNA. Genes Dev. 6, 1173-1189.
8. Baudin, A., Ozier, K.O., Denouel, A., Lacroute, F., and Cullin, C. (1993). A simple and efficient method for direct gene deletion in Saccharomyces cerevisiae. Nucleic Acids Res. 21, 3329-3330.
9. Belanger, K.D., Kenna, M.A., Wei, S., and Davis, L.I. (1994). Genetic and physical interactions between Srplp and nuclear pore complex proteins Nup1p and Nup2p. J. Cell Biol. 126, 619-630.
10. Belhumeur, P., Lee, A., Tam, R., DiPaolo, T., Fortin, N., and Clark, M.W. (1993). GSP1 and GSP2, genetic suppressors of the prp20-1 mutant in Saccharomyces cerevisiae: GTP-binding proteins involved in the maintenance of nuclear organization. Mol. Cell. Biol. 13, 2152-2161.
11. Bender, A., and Pringle, J.R. (1991). Use of a screen for synthetic lethal and multicopy suppressee mutants to identify two new genes involved in morphogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol. 11, 1295-1305.
12. Bischoff, F.R., Krebber, H., Kempf, T., Hermes, I., and Ponstingl, H. (1995). Human RanGTPase-activating protein RanGAP1 is a homologue of yeast Rna1p involved in mRNA processing and transport. Proc. Natl. Acad.Sci. USA 92, 1749-1753.
13. Bischoff, F.R., and Ponstingl, H. (1991a). Catalysis of guanine nucleotide exchange on Ran by the mitotic regulator RCC1. Nature 354, 80-82.
14. Bischoff, F.R., and Ponstingl, H. (1991b). Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide. Proc. Natl. Acad. Sci. USA 88, 10830-10834.
15. Bogerd, A.M., Hoffman, J.A., Amberg, D.C., Fink, G.R., and Davis, L.I. (1994). nup1 mutants exhibit pleiotropic defects in nuclear pore complex function. J. Cell Biol. 127, 319-332.
16. Bogerd, H.P., Fridell, R.A., Madore, S., and Cullen, B.R. (1995). Identification of a novel cellular cofactor for the Rev/Rex class of retroviral regulatory proteins. Cell 82, 485-494.
17. Breeden, L., and Nasmyth, K. (1985). Regulation of the yeast HO gene. Cold Spring Harbor Symp. Quant. Biol. 50, 643-650.
18. + RNA export and in the cytoskeleton. J. Biol. Chem. 270, 7411-7419.
19. Byers, B., and Goetsch, L. (1991). Preparation of yeast cells for thin-section electron microscopy. Methods Enzymol. 194, 602-608.
20. Cheng, Y., Dahlberg, J.E., and Lund, E. (1995). Diverse effects of the guanine nucleotide exchange factor RCC1 on RNA transport. Science 267, 1807-1810.
21. Chi, N.C., Adam, E.J., and Adam, S.A. (1995). Sequence and characterization of cytoplasmic nuclear protein import factor p97. J. Cell Biol. 130, 265-274.
22. Corbett, A.H., Koepp, D.M., Schlenstedt, G., Lee, M.S., Hopper, A.K., and Silver, P.A. (1995). Rna1p, a Ran/TC4 GTPase activating protein, is required for nuclear import. J. Cell Biol. 130, 1017-1026.
23. Daly, T.J., Cook, K.S., Gray, G.S., Maione, T.E., and Rusche, J.R. (1989). Specific binding of HIV-1 recombinant Rev protein to the Rev-responsive element in vitro. Nature 342, 816-819.
24. Davis, L.I. (1995). The nuclear pore complex. Annu. Rev. Biochem. 64, 865-896.
25. Davis, L.I., and Blobel, G. (1986). Identification and characterization of a nuclear pore complex protein. Cell 45, 699-709.
26. Davis, L.I., and Fink, G.R. (1990). The NUP1 gene encodes an essential component of the yeast nuclear pore complex. Cell 61, 965-978.
27. Dayhoff, M.O., Barker, W.C., and Hunt, L.T. (1983). Establishing homologies in protein sequences. Methods Enzymol. 91, 524-545.
28. Dingwall, C., and Laskey, R.A. (1991). Nuclear targeting sequences - a consensus? Trends Biochem. Sci. 16, 478-481.
29. Doye, V., and Hurt, E.C. (1995). Genetic approaches to nuclear pore structure and function. Trends Genet. 11, 235-241.
30. + RNA transport and nuclear pore distribution. EMBO J. 13, 6062-6075.
31. Enenkel, C., Blobel, G., and Rexach, M. (1995). Identification of a yeast karyopherin heterodimer that targets import substrate to mammalian nuclear pore complexes. J. Biol. Chem. 270, 16499-16502.
32. Fabre, E., Boelens, W.C., Wimmer, C., Mattaj, I.W., and Hurt, E.C. (1994). Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA in vitro via a novel conserved motif. Cell 78, 275-289.
33. Fields, S., and Song, O. (1989). A novel genetic system to detect protein-protein interactions. Nature 340, 245-246.
34. Fischer, U., Huber, J., Boelens, W.C., Mattaj, I.W., and Luhrmann, R. (1995). The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82, 475-483.
35. Forbes, D.J. (1992). Structure and function of the nuclear pore complex. Annu. Rev. Cell. Biol. 8, 495-527.
36. Forrester, W., Stutz, F., Rosbash, M., and Wickens, M. (1992). Defects in mRNA 3′-end formation, transcription initiation, and mRNA transport associated with the yeast mutation prp20: possible coupling of mRNA processing and chromatin structure. Genes Dev. 6, 1914-1926.
37. Fridell, R.A., Fischer, U., Luhrmann, R., Meyer, B.E., Meinkoth, J.L., Malim, M.H., and Cullen, B.R. (1996). Amphibian transcription factor IIIA proteins contain a sequence element functionally equivalent to the nuclear export signal of human immunodeficiency virus type 1 Rev. Proc. Natl. Acad. Sci. USA 93, 2936-2940.
38. Fritz, C.C., Zapp, M.L., and Green, M.R. (1995). A human nucleoporin-like protein that specifically interacts with HIV Rev. Nature 376, 530-533.
39. Gerace, L. (1995). Nuclear export signals and the fast track to the cytoplasm. Cell 82, 341-344.
40. Goldstein, A.L., Snay, C.A., Heath, C.V., and Cole, C.N. (1996). Pleiotropic nuclear defects associated with a conditional allele of the novel nucleoporin Rat9p/Nup85p. Mol. Biol. Cell 7, 917-934.
41. Gorlich, D., Kostka, S., Kraft, R., Dingwall, C., Laskey, R.A., Hartmann, E., and Prehn, S. (1995). Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Current Biol. 5, 383-392.
42. Gorlich, D., and Mattaj, I.W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518.
43. Gorlich, D., Prehn, S., Laskey, R.A., and Hartmann, E. (1994). Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778.
44. Gorlich, D., Vogel, F., Mills, A.D., Hartmann, E., and Laskey, R.A. (1995). Distinct functions for the two importin subunits in nuclear protein import. Nature 377, 246-248.
45. Gorsch, L.C., Dockendorff, T.C., and Cole, C.N. (1995). A conditional allele of the novel repeat-containing yeast nucleoporin RAT7/ NUP159 causes both rapid cessation of mRNA export and reversible clustering of nuclear pore complexes. J. Cell Biol. 129, 939-955.
46. Grandi, P., Schlaich, N., Tekotte, H., and Hurt, E.C. (1995). Functional interaction of Nic96p with a core nucleoporin complex consisting of Nsp1p, Nup49p and a novel protein Nup57p. EMBO J. 14, 76-87.
47. Hardy, C.F.J. (1996). OAF1, an essential ORC2 associated factor, plays a role in DNA replication. Mol. Cell. Biol. 16, 1832-1841.
48. + RNA associated with mutation of the Saccharomyccs cerevisiae rat2/nup120 gene. J. Cell Biol. 131, 1677-1697.
49. Henriquez, R., Blobel, G., and Aris, J.P. (1990). Isolation and sequencing of NOP1. A yeast gene encoding a nucleolar protein homologous to a human autoimmune antigen. J. Biol. Chem. 265, 2209-2215.
50. Hopper, A.K., Traglia, H.M., and Dunst, R.W. (1990). The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus. J. Cell Biol. 111, 309-321.
51. Iovine, M.K., Watkins, J.L., and Wente, S.R. (1995). The GLFG repetitive region of the nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor. J. Cell Biol. 131, 1699-1713.
52. Ito, H., Fukuda, Y., Murata, K., and Kimura, A. (1983). Transformation of intact yeast cells treated with alkali cations. J. Bacteriol. 153, 163-168.
53. Izaurralde, E., and Mattaj, I.W. (1995). RNA export. Cell 81, 153-159.
54. Jordan, E.G., Severs, N.J., and Williamson, D.H. (1977). Nuclear pore formation and the cell cycle in Saccharomyces cerevisiae. Exp. Cell Res. 104, 446-449.
55. Kadowaki, T., Chen, S., Hitomi, M., Jacobs, E., Kumagai, C., Liang, S., Schneiter, R., Singleton, D., Wisniewska, J., and Tartakoff, A.M. (1994). Isolation and characterization of Saccharomyces cerevisiae mRNA transport-defective (mtr) mutants. J. Cell Biol. 126, 649-659.
56. Kadowaki, T., Goldfarb, D., Spitz, L.M., Tartakoff, A.M. and Ohno, M. (1993). Regulation of RNA processing and transport by a nuclear guanine nucleotide release protein and members of the Ras superfamily. EMBO J. 12, 2929-2937.
57. Kadowaki, T., Zhao, Y., and Tartakoff, A.M. (1992). A conditional yeast mutant deficient in mRNA transport from nucleus to cytoplasm. Proc. Natl. Acad. Sci. USA 89, 2312-2316.
58. Koepp, D.M., Wong, D.H., Corbett, A.H., and Silver, P.A. (1996). Dynamic interactions of the nuclear import receptor and its interactions with transport factors. J. Cell Biol. 133, 1163-1176.
59. Lawrence, C.W. (1991). Classical mutagenesis techniques. Methods Enzymol. 194, 273-280.
60. + RNA and constitutive clustering of nuclear pore complexes. Mol. Biol. Cell 6, 401-417.
61. Loeb, J.D., Schlenstedt, G., Pellman, D., Kornitzer, D., Silver, P.A., and Fink, G.R. (1995). The yeast nuclear import receptor is required for mitosis. Proc. Natl. Acad. Sci. USA 92, 7647-7651.
62. Malim, M.H., Hauber, J., Le, S.-Y., Maizel, J.V., and Cullen, B.R. (1989). The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 338, 254-257.
63. Melchior, F., and Gerace, L. (1995). Mechanisms of nuclear protein import. Curr. Opin. Cell Biol. 7, 310-318.
64. Melchior, F., Paschal, B., Evans, J., and Gerace, L. (1993). Inhibition of nuclear protein import by nonhydrolyzable analogues of GTP and identification of the small GTPase Ran/TC4 as an essential transport factor. J. Cell Biol. 123, 1649-1659.
65. Meyer, B.E., and Malim, M.H. (1994). The HIV-1 Rev trans-activator shuttles between the nucleus and the cytoplasm. Genes Dev. 8, 1538-1547.
66. Michael, W.M., Choi, M., and Dreyfuss, G. (1995). A nuclear export signal in hnRNP A1: a signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83, 415-422.
67. Moore, M.S., and Blobel, G. (1993). The GTP-binding protein Ran/ TC4 is required for protein import into the nucleus. Nature 365, 661-663.
68. Moore, M.S., and Blobel, G. (1994). A G protein involved in nucleocytoplasmic transport: the role of Ran. Trends Biochem. Sci. 19, 211-216.
69. Moroianu, J., Blobel, G., and Radu, A. (1995a). Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes. Proc. Natl. Acad. Sci. USA 92, 2008-2011.
70. Moroianu, J., Hijikata, M., Blobel, G., and Radu, A. (1995b). Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins. Proc. Natl. Acad. Sci. USA 92, 6532-6536.
71. Murphy, R., and Wente, S.R. (1996). An RNA export mediator with a Rev-like nuclear export signal. Nature 382, 357-360.
72. Newmeyer, D.D., and Forbes, D.J. (1988). Nuclear import can be separated into distinct steps: in vitro nuclear pore binding and translocation. Cell 52, 641-653.
73. Pemberton, L.F., Rout, M.P., and Blobel, G. (1995). Disruption of the nucleoporin gene NUP133 results in clustering of nuclear pore complexes. Proc. Natl. Acad. Sci. USA 92, 1187-1191.
74. Pinol-Roma, S., and Dreyfuss, G. (1992). Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355, 730-732.
75. Powers, M.A., and Forbes, D.J. (1994). Cytosolic factors in nuclear transport: what's importin? Cell 79, 931-934.
76. Radu, A., Blobel, G., and Moore, M.S. (1995a). Identification of a protein complex that is required for nuclear protein import and mediates docking of import substrate to distinct nucleoporins. Proc. Natl. Acad. Sci. USA 92, 1769-1773.
77. Radu, A., Moore, M.S., and Blobel, G. (1995b). The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex. Cell 81, 215-222.
78. Richardson, W.D., Mills, A.D., Dilworth, S.M., Laskey, R.A., and Dingwall, C. (1988). Nuclear protein migration involves two steps: rapid binding at the nuclear envelope followed by slower translo-cation through nuclear pores. Cell 52, 655-664.
79. Rothstein, R. (1991). Targeting, disruption, replacement, and allele rescue: integrative DNA transformation in yeast. Methods Enzymol. 194, 281-301.
80. Rout, M.P., and Blobel, G. (1993). Isolation of the yeast nuclear pore complex. J. Cell Biol. 123, 771-783.
81. Rout, M.P., and Wente, S.R. (1994). Pores for thought: nuclear pore complex proteins. Trends Cell Biol. 4, 357-365.
82. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
83. Sanger, F., Nicklen, S., and Coulson, A.R. (1977). DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74, 5463-5467.
84. Schlenstedt, G., Hurt, E., Doye, V., and Silver, P.A. (1993). Reconstitution of nuclear protein transport with semi-intact yeast cells. J. Cell Biol. 123, 785-798.
85. Schlenstedt, G., Saavedra, C., Loeb, J.D., Cole, C.N., and Silver, P.A. (1995). The GTP-bound form of the yeast Ran/TC4 homologue blocks nuclear protein import and appearance of poly(A)+ RNA in the cytoplasm. Proc. Natl. Acad. Sci. USA 92, 225-229.
86. Severs, N.J., Jordan, E.G., and Williamson, D.H. (1976), Nuclear pore absence from areas of close association between nucleus and vacuole in synchronous yeast cultures. J. Ultrastruct. Res. 54, 374-387.
87. Sherman, F., Fink, G.R., and Hicks, J.B. (1986). Methods in Yeast Genetics, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
88. Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27.
89. Simos, G., and Hurt, E.C. (1995). Nucleocytoplasmic transport: factors and mechanisms. FEBS Lett. 369, 107-112.
90. Siniossoglou, S., Wimmer, C., Rieger, M., Doye, V., Tekotte, H., Weise, C., Emig, S., Segref, A., and Hurt, E.C. (1996). A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84, 265-275.
91. Stutz, F., Neville, M., and Rosbash, M. (1995). Identification of a novel nuclear pore-associated protein as a functional target of the HIV-1 Rev protein in yeast. Cell 82, 495-506.
92. Weis, K., Mattaj, I.W., and Lamond, A.I. (1995). Identification of hSRP1 alpha as a 0unctional receptor for nuclear localization sequences. Science 268, 1049-1053.
93. Wen, W., Meinkoth, J.L., Tsien, R.Y., and Taylor, S.S. (1995). Identification of a signal for rapid export of proteins from the nucleus. Cell 82, 463-473.
94. Wente, S.R., and Blobel, G. (1993). A temperature-sensitive NUP116 null mutant forms a nuclear envelope seal over the yeast nuclear pore complex thereby blocking nucleocytoplasmic traffic. J. Cell Biol. 123, 275-284.
95. Wente, S.R., and Blobel, G. (1994). NUP145 encodes a novel yeast glycine-leucine-phenylalanine-glycine (GLFG) nucleoporin required for nuclear envelope structure. J. Cell Biol. 125, 955-969.
96. Wente, S.R., Rout, M.P., and Blobel, G. (1992). A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119, 705-723.
97. Wimmer, C., Doye, V., Grandi, P., Nehrbass, U., and Hurt, E.C. (1992). A new subclass of nucleoporins that functionally interact with nuclear pore protein NSP1. EMBO J. 11, 5051-5061.
98. Yaffe, M.P., and Schatz, G. (1984). Two nuclear mutations that block mitochondrial protein import in yeast. Proc. Natl. Acad. Sci. USA 81, 4819-4823.
99. Yano, R., Oakes, M., Yamaghishi, M., Dodd, J.A., and Nomura, M. (1992). Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae. Mol. Cell. Biol. 12, 5640-5651.
100. Zapp, M.L., and Green, M.R. (1989). Sequence-specific RNA binding by the HIV-1 Rev protein. Nature 342, 714-716.