Nuclear import in permeabilized protoplasts from higher plants has unique features

Plant Cell

Volumn 8, Issue 8, 1996, Pages 1337-1352

  Hicks, Glenn R ^a   Smith, Harley M S ^a   Lobreaux, Stephane ^a,b   Raikhel, Natasha V ^a  

^a MICHIGAN STATE UNIVERSITY   (United States)

^b CNRS   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; EMBRYOPHYTA; NICOTIANA TABACUM; TRITICUM AESTIVUM; VERTEBRATA;

EID: 0030221054     PISSN: 10404651     EISSN: None     Source Type: Journal    
DOI: 10.1105/tpc.8.8.1337     Document Type: Article

References (76)

1. Ach, R.A., and Gruissem, W. (1994). A small nuclear GTP-binding protein from tomato suppresses a Schizosaccharomyces pombe cell cycle mutant. Proc Natl. Acad. Sci. USA 91, 5863-5867.
2. Adam, E.J.H., 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.
3. Adam, S.A. (1995). The importance of importin. Trends Cell Biol. 5, 189-191.
4. Adam, S.A., and Gerace, L. (1991). Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import. Cell 66, 837-847.
5. Adam, S.A., Lobl, T.J., Mitchell, M.A., and Gerace, L. (1989). Identification of specific binding proteins for a nuclear location sequence Nature 337, 276-279.
6. Adam, S.A., Sterne-Marr, R., and Gerace, L. (1990). Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors. J. Cell Biol. 111, 807-816.
7. Agutter, P.S., and Prochnow, D. (1994). Nucleocytoplasmic transport. Biochem. J. 300, 609-618.
8. Azuma, Y., Tabb, M.M., Vu, L., and Nomura, M. (1995). Isolation of a yeast protein kinase that is activated by the protein encoded by SRP1 (Srp1p) and phospharylates Srp1p complexed with nuclear localization signal peptides. Proc. Natl. Acad. Sci. USA 92, 5159-5163.
9. Boehm, U., Heinlein, M., Berhens, U., and Kunze, R. (1995) One of three nuclear localization signals of maize activator (Ac) transposase overlaps the DNA-binding domain. Plant J. 7, 441-451.
10. Boulikas, T. (1993). Nuclear localization signals (NLS). Cnt. Rev. Eukaryotic Gene Expression 3, 193-227.
11. Boulikas, T. (1994). Putative nuclear localization signals (NLS) in protein transcription factors. J. Cell Biochem. 55, 32-58.
12. Chi, N.C., Adam, E.J.H., and Adam, S.A. (1995). Sequence and characterization of cytoplasmic nuclear protein import factor p97. J. Cell Biol. 130, 265-274.
13. Cortes, P., Ye, Z.-S., and Baltimore, D. (1994). RAG-1 interacts with the repeated amino acid motif of the human homologue of the yeast protein SRP1. Proc. Natl. Acad. Sci. USA 91, 7633-7637.
14. Cuomo, C.A., Kirch, S., Gyuris, J., Brent, R., and Oettinger, M.A. (1994) Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein. Proc. Natl. Acad. Sci. USA 91, 6156-6160.
15. Davis, L.I. (1995) The nuclear pore complex. Annu. Rev. Biochem. 64, 865-896.
16. Dingwall, C., and Laskey, R. (1991). Nuclear targeting sequences-A consensus? Trends Biochem. Sci. 16, 478-481.
17. Dingwall, C., Kandels-Lewis, S., and Seraphin, B. (1995). A family of Ran binding proteins that includes nucleoporins. Proc. Natl. Acad. Sci. USA 92, 7525-7529.
18. Enenkel, C., Blobel, G., and Rexach, M. (1995). Identification of a yeast karyopherin heterodimer that targets import substrates to mammalian nuclear pore complexes J. Biol. Chem. 270, 16499-16502.
19. Finlay, D.R., Newmeyer, D.D., Price, T.M., and Forbes, D.J. (1987). Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores J Cell Biol. 104, 189-200.
20. Forbes, D.J. (1992) Structure and function of the nuclear pore complex. Annu. Rev. Cell Biol. 8, 495-527.
21. Gorlich, D., and Mattaj, I.W. (1996). Nucleocytoplasmic transport. Science 271, 1513-1518
22. 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.
23. Gorlich, D., Kostka, S., Kraft, R., Dingwall, C., Laskey, R.A., Hartmann, E., and Prehn, S. (1995a). Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope Curr Biol 5, 383-392
24. Gorlich, D., Vogel, F., Mills, A.D., Hartmann, E., and Laskey, R.A. (1995b). Distinct functions for the two importin subunits in nuclear protein import. Nature 377, 246-248.
25. Gorlich, D., Henklein, P., Laskey, R.A., and Hartmann, E. (1996). A 41 amino acid motif in importin-α confers binding to importin-β and hence transit into the nucleus. EMBO J. 15, 1810-1817.
26. Griesbach, R.J., and Sink, K.C. (1983). Evacuolation of mesophyll protoplasts. Plant Sci. Lett. 30, 297-301.
27. Harter, K., Kircher, S., Frohnmeyer, H., Krenz, M., Nagy, F., and Schäfer, E. (1994). Light-regulated modification and nuclear translocation of cytosolic G-box binding factors in parsley. Plant Cell 6, 545-559.
28. Heese-Peck, A., Cole, R.N., Borkhsenious, O.N., Hart, G.W., and Raikhel, N.V. (1995) Nuclear pore complex proteins from higher plants are modified by novel O-linked oligosaccharides. Plant Cell 7, 1459-1471.
29. Henikoff, S. (1987). Unidirectional digestion with exonuclease III in DNA sequence analysis. Methods Enzymol. 155, 156-165.
30. Hicks, G.R., and Raikhel, N.V. (1993). Specific binding of nuclear localization sequences to plant nuclei. Plant Cell 5, 983-994.
31. Hicks, G.R., and Raikhel, N.V. (1995a) Nuclear localization signal binding proteins in higher plant nuclei. Proc. Natl. Acad. Sci USA 92, 734-738.
32. Hicks, G.R., and Raikhel, N.V. (1995b) Protein import into the nucleus: An integrated view. Annu. Rev. Cell Dev. Biol 11, 155-188.
33. Hicks, G.R., Smith, H.M.S., Shieh, M., and Raikhel, N.V. (1995). Three classes of nuclear import signals bind to plant nuclei. Plant Physiol. 107, 1055-1058.
34. Hortensteiner, S., Martinoia, E., and Amrhein, N. (1994) Factors affecting the re-formation of vacuoles in evacuolated protoplasts and the expression of the two vacuolar proton pumps Planta 192, 395-403.
35. Imamoto, N., Matsuoka, Y., Kurihara, T., Kohno, K., Miyagi, M., Sakiyama, F., Okada, Y., Tsunasawa, S., and Yoneda, Y. (1992). Antibodies against 70-kD heat shock cognate protein inhibit mediated nuclear import of karyophilic proteins J Cell Biol. 119, 1047-1061
36. Imamoto, N., Shimamoto, T., Kose, S., Takao, T., Tachibana, T., Matsubae, M., Sekimoto, T., Shimonishi, Y., and Yoneda, Y. (1995a) The nuclear pore-targeting complex binds to nuclear pores after association with a karyophile. FEBS Lett. 368, 415-419.
37. Imamoto, N., Shimamoto, T., Takao, T., Tachibana, T., Kose, S., Matsubae, M., Sekimoto, T., Shimonishi, Y., and Yoneda, Y. (1995b). In vivo evidence for involvement of a 58 RDa component of nuclear pore-targeting complex in nuclear protein import. EMBO J. 14, 3617-3626.
38. Iovine, M.K., Watkins, J.L., and Wente, S.R. (1995). The GLFG repetitive region of nucleoporin Nup116p interacts with Kap95p, an essential yeast nuclear import factor J. Cell Biol. 131, 1699-1713.
39. Jans, D.A. (1995). The regulation of protein transport to the nucleus by phosphorylation. Biochem. J 311, 705-716.
40. Knorpp, C., Hugosson, M., Sjoling, S., Eriksson, A.C., and Glaser, E. (1994). Tissue-specific differences of the mitochondrial protein import machinery. In vitro import, processing and degradation of the pre-Fβ subunit of the ATP synthase in spinach leaf and root mitochondria. Plant Mol. Biol. 26, 571-579
41. Kotzin, B.L., Lafferty, J.A., Potanova, J.P., Rubin, R.L., and Tan, E.M. (1984). Monoclonal anti-histone autoantibodies derived from murine models of lupus. J. Immunol. 133, 2554-2559.
42. Kussel, P., and Frasch, M. (1995). Pendulin, a Drosophila protein with cell cycle-dependent nuclear localization, is required for normal cell proliferation. J. Cell Biol. 129, 1491-1507.
43. Leheny, E.A., and Theg, S.M. (1994). Apparent inhibition of chloroplast protein import by cold temperatures is due to energetic considerations not membrane fluidity. Plant Cell 6, 427-437.
44. 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.
45. Melchior, F., and Gerace, L. (1995). Mechanisms of nuclear protein import Curr. Opin Cell Biol. 7, 310-318.
46. Melchoir, 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.
47. Melchoir, F., Guan, T., Yokoyama, N., Nishimoto, T., and Gerace, L. (1995). GTP hydrolysis by Ran occurs at the nuclear pore complex in an early step of protein import. J. Cell Biol. 131, 571-581.
48. Merkle, T., Haizel, T., Matsumoto, T., Harter, K., Dallmann, G., and Nagy, F. (1994). Phenotype of the fission yeast cell cycle regulatory mutant pim1-46 is suppressed by a tobacco cDNA encoding a small, Ran-like GTP-binding protein. Plant J. 6, 555-565.
49. Miller, M.W., and Hanover, J.A. (1994). Functional nuclear pores reconstituted with β1-4 galactose-modified O-linked N-acetylglucosamine glycoproteins. J. Biol. Chem. 269, 9289-9297.
50. 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.
51. Moore, M.S., and Blobel, G. (1994). Purification of a Ran-interacting protein that is required for protein import into the nucleus. Proc. Natl. Acad. Sci. USA 91, 10212-10216.
52. 2 subunit binds nuclear localization signal and β subunit interacts with peptide repeat-containing nucleoporins Proc. Natl Acad. Sci. USA 92, 6532-6536.
53. Nehrbass, U., and Blobel, G. (1996). Role of the nuclear transport factor p10 in nuclear import. Science 272, 120-122.
54. Newman, T., de Bruijn, F.J., Green, P., Keegstra, K., Kende, H., McIntosh, L., Ohlrogge, J., Raikhel, N., Somerville, S., Thomashow, M., Retzel, E., and Somerville, C. (1994). Genes galore A summary of methods for accessing results from large-scale partial sequencing of anonymous Arabidopsis cDNA clones. Plant Physiol. 106, 1241-1255.
55. Newmeyer, D.D., Finlay, D.R., and Forbes, D.J. (1986). In vitro transport of a fluorescent nuclear protein and exclusion of non-nuclear proteins. J. Cell Biol 103, 2091-2102.
56. Paschal, B.M., and Gerace, L. (1995). Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62. J. Cell Biol. 129, 925-937.
57. Reifer, M., Berg, S., and Reynolds, A.B. (1994). A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 76, 789-791.
58. Perata, P., Pozueta-Romero, J., Yamaguchi, J., and Akazawa, T. (1992). Artifactual detection of ADP-dependent sucrose synthase in crude plant extracts FEBS Lett. 3, 283-287.
59. Pruschy, M., Ju, Y., Spitz, L., Carafoli, E., and Goldfarb, D.S. (1994). Facilitated nuclear transport of calmodulin in tissue culture cells. J. Cell Biol 127, 1527-1536.
60. 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.
61. 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
62. Rexach, M., and Blobel, G. (1996). Protein import into nuclei: Association and dissociation reactions involving transport substrate, transport factors, and nucleoporins. Cell 83, 683-692.
63. Sambrook, J., Fritsch, E.F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed. (Cold Spring Harbor, NY: Cold Spring Harbor Laboratory).
64. 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.
65. + RNA in the cytoplasm. Proc. Natl. Acad. Sci USA 92, 225-229.
66. Shi, Y., and Thomas, J.O. (1992). The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol. Cell Biol 12, 2186-2192.
67. Siomi, H., and Dreyfuss, G. (1995). A nuclear localization domain in the hnRNP A1 protein. J. Cell Biol. 129, 551-560.
68. Smith, E.F., and Lefebvre, P.A. (1996). PF16 encodes a protein with armadillo repeats and localizes to a single microtubule of the central apparatus in Chlamydomonas flagella. J. Cell Biol. 132, 359-370.
69. Torok, I., Strand, D., Schmitt, R., Tick, G., Torok, T., Kiss, I., and Mechler, B.M. (1995) The overgrown hematopoietic organs-31 tumor suppressor gene of Drosophila encodes an importin-like protein accumulating in the nucleus at the onset of mitosis. J. Cell Biol. 129, 1473-1489.
70. Varagona, M.J., and Raikhel, N.V. (1994). The basic domain in the bZIP regulatory protein Opaque2 serves two independent functions: DNA binding and nuclear localization. Plant J. 2, 207-214.
71. Weis, K., Mattaj, I.W., and Lamond, A.I. (1995). Identification of hSRP1α as a functional receptor for nuclear localization sequences. Science 268, 1049-1053.
72. Weis, K., Ryder, U., and Lamond, A.I. (1996). The conserved amino-terminal domain of hSRP1 α is essential for nuclear protein import. EMBO J 15, 1818-1825
73. Wu, J., Matunis, M.J., Kraemer, D., Blobel, G., and Coutavas, E. (1995). Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. J. Biol. Chem. 270, 14209-14213.
74. Yano, R., Oakes, M.L., Yamaghishi, M., Dodd, J.A., and Nomura, M. (1992). Cloning and characterization of SRP1, a suppressor of temperature-sensitive RNA polymerase 1 mutations, in Saccharomyces cerevisias. Mol. Cell. Biol. 12, 5640-5651.
75. Yokoyama, N., Hayashi, N., Seki, T., Pante, N., Ohba, T., Nishii, K., Kuma, K., Hayashida, T., Miyata, T., Aebi, U, Fukui, M., and Nishimoto, T. (1995). A giant nucleopore protein that binds Ran/TC4. Nature 376, 184-188.
76. Zupan, J.R., Citovsky, V., and Zambryski, P. (1996). Agrobacterium VirE2 protein mediates nuclear uptake of single-stranded DNA in plant cells. Proc Natl. Acad. Sci. USA 93, 2392-2397.