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Nuclear Import and Export in Plants and Animals pp 83–99Cite as

Nuclear Import of Agrobacterium T-DNA

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Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

Abstract

Agrobacterium-mediated genetic transformation is a process by which genetic material is transported from the bacterium into the host nucleus, where it stably integrates. The transferred DNA (T-DNA) is escorted, by two bacterial proteins, as a single-stranded DNA-protein complex (a T-complex), which mediate its transport to the host nucleus. The large size and mass of this DNA-protein complex raise questions as to the molecular machinery and mechanism by which the T-complex passes the nuclear pore barrier. Recent studies have revealed the important role of specific host proteins in interacting with and guiding the T-complex through the nuclear pore, and to its point of integration. In this chapter, we summarize our knowledge of the function of T-DNA bacterial and host protein chaperones, and draw a model for their action during the nuclear import and intranuclear transport of Agrobacterium T-DNA.

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References

  1. Gelvin SB. Agrobacterium and plant genes involved in T-DNA transfer and integration. Annu Rev Plant Physiol Plant Mol Biol 2000; 51:223–256.

    PubMed  CAS  Google Scholar 

  2. Gelvin SB. Agrobacterium-mediated plant transformation: The biology behind the “gene-jockeying” tool. Microbiol Mol Biol Rev 2003; 67:16–37.

    PubMed  CAS  Google Scholar 

  3. Tzfira T, Citovsky V. From host recognition to T-DNA integration: The function of bacterial and plant genes in the Agrobacterium-plant cell interaction. Mol Plant Pathol 2000; 1:201–212.

    CAS  Google Scholar 

  4. Tzfira T, Citovsky V. Partners-in-infection: Host proteins involved in the transformation of plant cells by Agrobacterium. Trends Cell Biol 2002; 12:121–129.

    PubMed  CAS  Google Scholar 

  5. Zupan J, Muth TR, Draper O et al. The transfer of DNA from Agrobacterium tumefaciens into plants: A feast of fundamental insights. Plant J 2000; 23:11–28.

    PubMed  CAS  Google Scholar 

  6. de Cleene M, de Ley J. The host range of crown gall. Bot Rev 1976; 42:389–466.

    Google Scholar 

  7. Piers KL, Heath JD, Liang X et al. Agrobacterium tumefaciens-mediated transformation of yeast. Proc Natl Acad Sci USA 1996; 93:1613–1618.

    PubMed  CAS  Google Scholar 

  8. de Groot MJ, Bundock P, Hooykaas PJJ et al. Agrobacterium tumefaciens-mediated transformation of filamentous fungi [published erratum appears in Nat Biotechnol 1998; 16:1074]. Nat Biotechnol 1998; 16:839–842.

    PubMed  Google Scholar 

  9. Gouka RJ, Gerk C, Hooykaas PJ et al. Transformation of Aspergillus awamori by Agrobacterium tumefaciens-mediated homologous recombination. Nat Biotechnol 1999; 17:598–601.

    PubMed  CAS  Google Scholar 

  10. Kunik T, Tzfira T, Kapulnik Y et al. Genetic transformation of HeLa cells by Agrobacterium. Proc Natl Acad Sci USA 2001; 98:1871–1876.

    PubMed  CAS  Google Scholar 

  11. Gelvin S. Improving plant genetic engineering by manipulating the host. Trends Biotechnol 2003; 21:95–98.

    PubMed  CAS  Google Scholar 

  12. Peralta EG, Ream LW. T-DNA border sequences required for crown gall tumorigenesis. Proc Natl Acad Sci USA 1985; 82:5112–5116.

    PubMed  CAS  Google Scholar 

  13. Wang K, Stachel SE, Timmerman B et al. Site-specific nick occurs within the 25 bp transfer promoting border sequence following induction of vir gene expression in Agrobacterium tumefaciens. Science 1987; 235:587–591.

    CAS  Google Scholar 

  14. Armitage P, Walden R, Draper J. Plant genetic transformation and gene expression. In: Draper J, Scott R, Armitage P et al, eds. A Laboratory Manual. London: Blackwell Scientific Publications Ltd., 1988:1–67.

    Google Scholar 

  15. Draper J, Scott R, Armitage P et al. Plant genetic transformation and gene expression. A Laboratory Manual. London: Blackwell Scientific Publications Ltd., 1988.

    Google Scholar 

  16. Lee YW, Jin S, Sim WS et al. The sensing of plant signal molecules by Agrobacterium: genetic evidence for direct recognition of phenolic inducers by the VirA protein. Gene 1996; 179:83–88.

    PubMed  CAS  Google Scholar 

  17. McLean BG, Greene EA, Zambryski PC. Mutants of Agrobacterium VirA that activate vir gene expression in the absence of the inducer acetosyringone. J Biol Chem 1994; 269:2645–2651.

    PubMed  CAS  Google Scholar 

  18. Stachel SE, Messens E, Van Montagu M et al. Identification of the signal molecules produced by wounded plant cell that activate T-DNA transfer in Agrobacterium tumefaciens. Nature 1985; 318:624–629.

    Google Scholar 

  19. Stachel SE, Nester EW, Zambryski PC. A plant cell factor induces Agrobacterium tumefaciens vir gene expression. Proc Natl Acad Sci USA 1986; 83:379–383.

    PubMed  CAS  Google Scholar 

  20. Turk SC, van Lange RP, Regensburg-Tuink TJG et al. Localization of the VirA domain involved in acetosyringone-mediated vir gene induction in Agrobacterium tumefaciens. Plant Mol Biol 1994; 25:899–907.

    PubMed  CAS  Google Scholar 

  21. Durrenberger F, Crameri A, Hohn B et al. Covalently bound VirD2 protein of Agrobacterium tumefaciens protects the T-DNA from exonucleolytic degradation. Proc Natl Acad Sci USA 1989; 86:9154–9158.

    PubMed  CAS  Google Scholar 

  22. Jasper F, Koncz C, Schell J et al. Agrobacterium T-strand production in vitro: sequence-specific cleavage and 5′ protection of single-stranded DNA templates by purified VirD2 protein. Proc Natl Acad Sci USA 1994; 91:694–698.

    PubMed  CAS  Google Scholar 

  23. Pansegrau W, Schoumacher F, Hohn B et al. Site-specific cleavage and joining of single-stranded DNA by VirD2 protein of Agrobacterium tumefaciens Ti plasmids: Analogy to bacterial conjugation. Proc Natl Acad Sci USA 1993; 90:11538–11542.

    PubMed  CAS  Google Scholar 

  24. Relic B, Andjelkovic M, Rossi L et al. Interaction of the DNA modifying proteins VirD1 and VirD2 of Agrobacterium tumefaciens: Analysis by subcellular localization in mammalian cells. Proc Natl Acad Sci USA 1998; 95:9105–9110.

    PubMed  CAS  Google Scholar 

  25. Scheiffele P, Pansegrau W, Lanka E. Initiation of Agrobacterium tumefaciens T-DNA processing: Purified proteins VirD1 and VirD2 catalyze site-and strand-specific cleavage of superhelical T-border DNA in vitro. J Biol Chem 1995; 270:1269–1276.

    PubMed  CAS  Google Scholar 

  26. Ward E, Barnes W. VirD2 protein of Agrobacterium tumefaciens very tightly linked to the 5′ end of T-strand DNA. Science 1988; 242:927–930.

    CAS  Google Scholar 

  27. Young C, Nester EW. Association of the VirD2 protein with the 5’ end of T-strands in Agrobacterium tumefaciens. J Bacteriol 1988; 170:3367–3374.

    PubMed  CAS  Google Scholar 

  28. Christie PJ, Ward JE, Winans SC et al. The Agrobacterium tumefaciens virE2 gene product is a single-stranded-DNA-binding protein that associates with T-DNA. J Bacteriol 1988; 170:2659–2667.

    PubMed  CAS  Google Scholar 

  29. Citovsky V, Wong ML, Zambryski PC. Cooperative interaction of Agrobacterium VirE2 protein with single stranded DNA: Implications for the T-DNA transfer process. Proc Natl Acad Sci USA 1989; 86:1193–1197.

    PubMed  CAS  Google Scholar 

  30. Sen P, Pazour GJ, Anderson D et al. Cooperative binding of Agrobacterium tumefaciens VirE2 protein to single-stranded DNA. J Bacteriol 1989; 171:2573–80.

    PubMed  CAS  Google Scholar 

  31. Vergunst AC, Schrammeijer B, den Dulk-Ras A et al. VirB/D4-dependent protein translocation from Agrobacterium into plant cells. Science 2000; 290:979–982.

    PubMed  CAS  Google Scholar 

  32. Zupan J, Ward D, Zambryski PC. Assembly of the VirB transport complex for DNA transfer from Agrobacterium tumefaciens to plant cells. Curr Opin Microbiol 1998; 1:649–655.

    PubMed  CAS  Google Scholar 

  33. Gheysen G, Villarroel R, Van Montagu M. Illegitimate recombination in plants: a model for T-DNA integration. Genes Dev 1991; 5:287–297.

    PubMed  CAS  Google Scholar 

  34. Mayerhofer R, Koncz-Kalman Z, Nawrath C et al. T-DNA integration: a mode of illegitimate recombination in plants. EMBO J 1991; 10:697–704.

    PubMed  CAS  Google Scholar 

  35. Takano M, Egawa H, Ikeda JE et al. The structures of integration sites in transgenic rice. Plant J 1997; 11:353–361.

    PubMed  CAS  Google Scholar 

  36. Tinland B. The integration of T-DNA into plant genomes. Trends Plant Sci 1996; 1:178–184.

    Google Scholar 

  37. Bakó L, Umeda M, Tiburcio AF et al. The VirD2 pilot protein of Agrobacterium-transferred DNA interacts with the TATA box-binding protein and a nuclear protein kinase in plants. Proc Natl Acad Sci USA 2003; 100:10108–10113.

    PubMed  Google Scholar 

  38. Mysore KS, Bassuner B, Deng XB et al. Role of the Agrobacterium tumefaciens VirD2 protein in T-DNA transfer and integration. Mol Plant-Microbe Interact 1998; 11:668–683.

    PubMed  CAS  Google Scholar 

  39. Dombek P, Ream LW. Functional domains of Agrobacterium tumefaciens single-stranded DNA-binding protein VirE2. J Bacteriol 1997; 179:1165–1173.

    PubMed  CAS  Google Scholar 

  40. Simone M, McCullen CA, Stahl LE et al. The carboxy-terminus of VirE2 from Agrobacterium tumefaciens is required for its transport to host cells by the virB-encoded type IV transport system. Mol Microbiol 2001; 41:1283–1293.

    PubMed  CAS  Google Scholar 

  41. Zhou XR, Christie PJ. Mutagenesis of the Agrobacterium VirE2 single-stranded DNA-binding pro tein identifies regions required for self-association and interaction with VirE1 and a permissive site for hybrid protein construction. J Bacteriol 1999; 181:4342–4352.

    PubMed  CAS  Google Scholar 

  42. Vergunst AC, van Lier MCM, den Dulk-Ras A et al. Recognition of the Agrobacterium VirE2 translocation signal by the VirB/D4 transport system does not require VirE1. Plant Physiol 2003; 133:978–988.

    PubMed  CAS  Google Scholar 

  43. Frary A, Hamilton CM. Efficiency and stability of high molecular weight DNA transformation: An analysis in tomato. Transgenic Res 2001; 10:121–132.

    PubMed  CAS  Google Scholar 

  44. Hamilton CM. A binary-BAC system for plant transformation with high-molecular-weight DNA. Gene 1997; 200:107–16.

    PubMed  CAS  Google Scholar 

  45. Kononov ME, Bassuner B, Gelvin SB. Integration of T-DNA binary vector ‘backbone’ sequences into the tobacco genome: Evidence for multiple complex patterns of integration. Plant J 1997; 11:945–57.

    PubMed  CAS  Google Scholar 

  46. Ramanathan V, Veluthambi K. Transfer of nonT-DNA portions of the Agrobacterium tumefaciens Ti plasmid pTiA6 from the left terminus of TL-DNA. Plant Mol Biol 1995; 28:1149–54.

    PubMed  CAS  Google Scholar 

  47. Wenck A, Czako M, Kanevski I et al. Frequent collinear long transfer of DNA inclusive of the whole binary vector during Agrobacterium-mediated transformation. Plant Mol Biol 1997; 34:913–22.

    PubMed  CAS  Google Scholar 

  48. Citovsky V, Zupan J, Warnick D et al. Nuclear localization of Agrobacterium VirE2 protein in plant cells. Science 1992; 256:1802–1805.

    PubMed  CAS  Google Scholar 

  49. Gelvin SB. Agrobacterium VirE2 proteins can form a complex with T strands in the plant cytoplasm. J Bacteriol 1998; 180:4300–4302.

    PubMed  CAS  Google Scholar 

  50. Sundberg C, Meek L, Carrol K et al. VirE1 protein mediates export of single-stranded DNA binding protein VirE2 from Agrobacterium tumefaciens into plant cells. J Bacteriol 1996; 178:1207–1212.

    PubMed  CAS  Google Scholar 

  51. Ward DV, Zambryski PC. The six functions of Agrobacterium VirE2. Proc Natl Acad Sci USA 2001; 98:385–386.

    PubMed  CAS  Google Scholar 

  52. Binns AN, Beaupre CE, Dale EM. Inhibition of VirB-mediated transfer of diverse substrates from Agrobacterium tumefaciens by the InQ plasmid RSF1010. J Bacteriol 1995; 177:4890–4899.

    PubMed  CAS  Google Scholar 

  53. Otten L, DeGreve H, Leemans J et al. Restoration of virulence of vir region mutants of A. tumefaciens strain B6S3 by coinfection with normal and mutant Agrobacterium strains. Mol Gen Genet 1984; 195:159–163.

    CAS  Google Scholar 

  54. Lee LY, Gelvin SB, Kado CI. pSa causes oncogenic suppression of Agrobacterium by inhibiting VirE2 protein export. J Bacteriol 1999; 181:186–196.

    PubMed  CAS  Google Scholar 

  55. Deng W, Chen L, Peng WT et al. VirE1 is a specific molecular chaperone for the exported single-stranded-DNA-binding protein VirE2 in Agrobacterium. Mol Microbiol 1999; 31:1795–1807.

    PubMed  CAS  Google Scholar 

  56. Sundberg CD, Ream LW. The Agrobacterium tumefaciens chaperone-like protein, VirE1, interacts with VirE2 at domains required for single-stranded DNA binding and cooperative interaction. J Bacteriol 1999; 181:6850–6855.

    PubMed  CAS  Google Scholar 

  57. Yusibov VM, Steck TR, Gupta V et al. Association of single-stranded transferred DNA from Agrobacterium tumefaciens with tobacco cells. Proc Natl Acad Sci USA 1994; 91:2994–2998.

    PubMed  CAS  Google Scholar 

  58. Citovsky V, Guralnick B, Simon MN et al. The molecular structure of Agrobacterium VirE2-single stranded DNA complexes involved in nuclear import. J Mol Biol 1997; 271:718–727.

    PubMed  CAS  Google Scholar 

  59. Hamilton CM, Frary AC, Lewis C et al. Stable transfer of intact high molecular weight DNA into plant chromosomes. Proc Natl Acad Sci USA 1996; 93:9975–9979.

    PubMed  CAS  Google Scholar 

  60. Forbes DJ. Structure and function of the nuclear pore complex. Annu Rev Cell Biol 1992; 8:495–527.

    PubMed  CAS  Google Scholar 

  61. Dworetzky SI, Feldherr CM. Translocation of RNA-coated gold particles through the nuclear pores of oocytes. J Cell Biol 1988; 106:575–584.

    PubMed  CAS  Google Scholar 

  62. Pante N, Kann M. Nuclear pore complex is able to transport macromolecules with diameters of about 39 nm. Mol Biol Cell 2002; 13:425–434.

    PubMed  CAS  Google Scholar 

  63. Briels WJ. The theory of polymer dynamics. Oxford: Clarendon Press, 1986.

    Google Scholar 

  64. Landau LD, Lifshitz EM. Statistical Physics. Oxford: Pergamon Press, 1980.

    Google Scholar 

  65. Fahrenkrog B, Aebi U. The nuclear pore complex: Nucleocytoplasmic transport and beyond. Nat Rev Mol Cell Biol 2003; 4:757–66.

    PubMed  CAS  Google Scholar 

  66. Suntharalingam M, Wente SR. Peering through the pore. Nuclear pore complex structure, assembly, and function. Dev Cell 2003; 4:775–789.

    PubMed  CAS  Google Scholar 

  67. Zambryski PC. Chronicles from the Agrobacterium-plant cell DNA transfer story. Annu Rev Plant Physiol Plant Mol Biol 1992; 43:465–490.

    CAS  Google Scholar 

  68. Howard E, Zupan J, Citovsky V et al. The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: Implications for nuclear uptake of DNA in plant cells. Cell 1992; 68:109–118.

    PubMed  CAS  Google Scholar 

  69. Tinland B, Schoumacher F, Gloeckler V et al. The Agrobacterium tumefaciens virulence D2 protein is responsible for precise integration of T-DNA into the plant genome. EMBO J 1995; 14:3585–3595.

    PubMed  CAS  Google Scholar 

  70. Ziemienowicz A, Merkle T, Schoumacher F et al. Import of Agrobacterium T-DNA into plant nuclei: Two distinct functions of VirD2 and VirE2 proteins. Plant Cell 2001; 13:369–384.

    PubMed  CAS  Google Scholar 

  71. Citovsky V, Warnick D, Zambryski PC. Nuclear import of Agrobacterium VirD2 and VirE2 proteins in maize and tobacco. Proc Natl Acad Sci USA 1994; 91:3210–3214.

    PubMed  CAS  Google Scholar 

  72. Herrera-Estrella A, Van Montagu M, Wang K. A bacterial peptide acting as a plant nuclear targeting signal: The amino-terminal portion of Agrobacterium VirD2 protein directs a beta-galactosidase fusion protein into tobacco nuclei. Proc Natl Acad Sci USA 1990; 87:9534–9537.

    PubMed  CAS  Google Scholar 

  73. Rossi L, Hohn B, Tinland B. The VirD2 protein of Agrobacterium tumefaciens carries nuclear localization signals important for transfer of T-DNA to plant. Mol Gen Genet 1993; 239:345–353.

    PubMed  CAS  Google Scholar 

  74. Tinland B, Koukolikova-Nicola Z, Hall MN et al. The T-DNA-linked VirD2 protein contains two distinct nuclear localization signals. Proc Natl Acad Sci USA 1992; 89:7442–7446.

    PubMed  CAS  Google Scholar 

  75. Tzfira T, Citovsky V. Comparison between nuclear import of nopaline-and octopine-specific VirE2 protein of Agrobacterium in plant and animal cells. Mol Plant Pathol 2001; 2:171–176.

    CAS  Google Scholar 

  76. Koukolikova-Nicola Z, Raineri D, Stephens K et al. Genetic analysis of the virD operon of Agrobacterium tumefaciens: A search for functions involved in transport of T-DNA into the plant cell nucleus and in T-DNA integration. J Bacteriol 1993; 175:723–731.

    PubMed  CAS  Google Scholar 

  77. Shurvinton CE, Hodges L, Ream LW. A nuclear localization signal and the C-terminal omega sequence in the Agrobacterium tumefaciens VirD2 endonuclease are important for tumor formation. Proc Natl Acad Sci USA 1992; 89:11837–11841.

    PubMed  CAS  Google Scholar 

  78. Narasimhulu SB, Deng X-B, Sarria R et al. Early transcription of Agrobacterium T-DNA genes in tobacco and maize. Plant Cell 1996; 8:873–886.

    PubMed  CAS  Google Scholar 

  79. Zupan J, Citovsky V, Zambryski PC. Agrobacterium VirE2 protein mediates nuclear uptake of ssDNA in plant cells. Proc Natl Acad Sci USA 1996; 93:2392–2397.

    PubMed  CAS  Google Scholar 

  80. Sheng J, Citovsky V. Agrobacterium-plant cell interaction: Have virulence proteins-will travel. Plant Cell 1996; 8:1699–1710.

    PubMed  CAS  Google Scholar 

  81. Tinland B, Hohn B. Recombination between prokaryotic and eukaryotic DNA: integration of Agrobacterium tumefaciens T-DNA into the plant genome. Genet Eng 1995; 17:209–229.

    CAS  Google Scholar 

  82. Windels P, De Buck S, Van Bockstaele E et al. T-DNA integration in Arabidopsis chromosomes. Presence and origin of filler DNA sequences. Plant Physiol 2003; 133:2061–2068.

    PubMed  CAS  Google Scholar 

  83. Guralnick B, Thomsen G, Citovsky V. Transport of DNA into the nuclei of Xenopus oocytes by a modified VirE2 protein of Agrobacterium. Plant Cell 1996; 8:363–373.

    PubMed  CAS  Google Scholar 

  84. Ziemienowicz A, Görlich D, Lanka E et al. Import of DNA into mammalian nuclei by proteins originating from a plant pathogenic bacterium. Proc Natl Acad Sci USA 1999; 96:3729–3733.

    PubMed  CAS  Google Scholar 

  85. Rhee Y, Gurel F, Gafni Y et al. A genetic system for detection of protein nuclear import and export. Nat Biotechnol 2000; 18:433–437.

    PubMed  CAS  Google Scholar 

  86. Tzfira T, Vaidya M, Citovsky V. VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2, is involved in VirE2 nuclear import and Agrobacterium infectivity. EMBO J 2001; 20:3596–3607.

    PubMed  CAS  Google Scholar 

  87. Williams RC, Spengler SJ. Fibers of RecA protein and complexes of RecA protein and single stranded fX174 DNA as visualized by negative-stain electron microscopy. J Mol Biol 1986; 192:110–118.

    Google Scholar 

  88. Flory J, Radding CM. Visualization of recA protein and its association with DNA: A priming effect of single-strand-binding protein. Cell 1982; 28:747–56.

    PubMed  CAS  Google Scholar 

  89. Flory J, Tsang SS, Muniyappa K. Isolation and visualization of active presynaptic filaments of recA protein and single-stranded DNA. Proc Natl Acad Sci USA 1984; 81:7026–30.

    PubMed  CAS  Google Scholar 

  90. Ballas N, Citovsky V. Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein. Proc Natl Acad Sci USA 1997; 94:10723–10728.

    PubMed  CAS  Google Scholar 

  91. Deng W, Chen L, Wood DW et al. Agrobacterium VirD2 protein interacts with plant host cyclophilins. Proc Natl Acad Sci USA 1998; 95:7040–7045.

    PubMed  CAS  Google Scholar 

  92. Fields S, Song O-K. A novel genetic system to detect protein-protein interactions. Nature 1989; 340:245–246.

    PubMed  CAS  Google Scholar 

  93. Hollenberg SM, Sternglanz R, Cheng PF et al. Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol Cell Biol 1995; 15:3813–3822.

    PubMed  CAS  Google Scholar 

  94. Duina AA, Chang HC, Marsh JA et al. A cyclophilin function in Hsp90-dependent signal transduction. Science 1996; 274:1713–1715.

    PubMed  CAS  Google Scholar 

  95. Fischer G, Wittmann-Liebold B, Lang K et al. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 1989; 337:476–478.

    PubMed  CAS  Google Scholar 

  96. Hayman GT, Miernyk JA. The nucleotide and deduced amino acid sequences of a peptidyl-prolyl cis-trans isomerase from Arabidopsis thaliana. Biochim Biophys Acta 1994; 1219:536–538.

    PubMed  CAS  Google Scholar 

  97. Hunter T. Prolyl isomerases and nuclear function. Cell 1998; 92:141–143.

    PubMed  CAS  Google Scholar 

  98. Lippuner V, Chou IT, Scott SV et al. Cloning and characterization of chloroplast and cytosolic forms of cyclophilin from Arabidopsis thaliana. J Biol Chem 1994; 269:7863–7868.

    PubMed  CAS  Google Scholar 

  99. Marks AR. Cellular functions of immunophilins. Physiol Rev 1996; 76:631–649.

    PubMed  CAS  Google Scholar 

  100. Takahashi N, Hayano T, Suzuki M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin. Nature 1989; 337:473–475.

    PubMed  CAS  Google Scholar 

  101. Handschumacher RE, Harding MW, Rice J et al. Cyclophilin: A specific cytosolic binding protein for cyclosporin A. Science 1984; 226:544–547.

    PubMed  CAS  Google Scholar 

  102. Baker EK, Colley NJ, Zuker CS. The cyclophilin homolog NinaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J 1994; 13:4886–4895.

    PubMed  CAS  Google Scholar 

  103. Meyer K, Leube MP, Grill E. A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana. Science 1994; 264:1452–1455.

    PubMed  CAS  Google Scholar 

  104. Leung J, Bouvier-Durand M, Morris P-C et al. Arabidopsis ABA response gene ABU: Features of a calcium-modulated protein phosphatase. Science 1994; 264:1448–1452.

    PubMed  CAS  Google Scholar 

  105. Nigg EA. Nucleocytoplasmic transport: Signals, mechanisms and regulation. Nature 1997; 386:779–787.

    PubMed  CAS  Google Scholar 

  106. Powers MA, Forbes DJ. Cytosolic factors in nuclear import: what’s importin? Cell 1994; 79:931–934.

    PubMed  CAS  Google Scholar 

  107. Peifer M, Berg S, Reynolds AB. A repeating amino acid motif shared by proteins with diverse cellular roles. Cell 1994; 76:789–791.

    PubMed  CAS  Google Scholar 

  108. Görlich D, Mattaj IW. Nucleocytoplasmic transport. Science 1996; 271:1513–1518.

    PubMed  Google Scholar 

  109. Loeb JDJ, Schlenstedt G, Pellman D et al. The yeast nuclear import receptor is required for mitosis. Proc Natl Acad Sci USA 1995; 92:7647–7651.

    PubMed  CAS  Google Scholar 

  110. Schlenstedt G, Hurt E, Doye V et al. Reconstitution of nuclear protein transport with semi-intact yeast cells. J Cell Biol 1993; 123:785–798.

    PubMed  CAS  Google Scholar 

  111. Zhu Y, Nam J, Humara JM et al. Identification of Arabidopsis rat mutants. Plant Physiol 2003; 132:494–505.

    PubMed  CAS  Google Scholar 

  112. Coin F, Frit P, Viollet B et al. TATA binding protein discriminates between different lesions on DNA, resulting in a transcription decrease. Mol Biol Cell 1998; 18:3907–3914.

    CAS  Google Scholar 

  113. Vichi P, Coin F, Renaud JP et al. Cisplatin-and UV-damaged DNA lure the basal transcription factor TFIID/TBP. Embo J 1997; 16:7444–56.

    PubMed  CAS  Google Scholar 

  114. Balajee AS, Bohr VA. Genomic heterogeneity of nucleotide excision repair. Gene 2000; 250:15–30.

    PubMed  CAS  Google Scholar 

  115. van der Krol AR, Chua N-H. The basic domain of plant B-ZIP proteins facilitates import of a reporter protein into plant nuclei. Plant Cell 1991; 3:667–675.

    PubMed  Google Scholar 

  116. Tzfira T, Vaidya M, Citovsky V. Increasing plant susceptibility to Agrobacterium infection by overexpression of the Arabidopsis VIP1 gene. Proc Natl Acad Sci USA 2002; 99:10435–10440.

    PubMed  CAS  Google Scholar 

  117. Avivi Y, Morad V, Ben-Meir H et al. Reorganization of specific chromosomal domains and activetion of silent genes in plant cell acquiring pluripotentiality. Dev Dyn 2004; in press.

    Google Scholar 

  118. Newell CA. Plant transformation technology. Developments and applications. Mol Biotechnol 2000; 16:53–65.

    PubMed  CAS  Google Scholar 

  119. Rakoczy-Trojanowska M. Alternative methods of plant transformation—a short review. Cell Mol Biol Lett 2002; 7:849–58.

    PubMed  Google Scholar 

  120. Pemberton LF, Rosenblum JS, Blobel G. Nuclear import of the TATA-binding protein: mediation by the karyopherin Kap114p and a possible mechanism for intranuclear targeting. J Cell Biol 1999; 145:1407–1417.

    PubMed  CAS  Google Scholar 

  121. Schrammeijer B, Dulk-Ras Ad A, Vergunst AC et al. Analysis of Vir protein translocation from Agrobacterium tumefaciens using Saccharomyces cerevisiae as a model: Evidence for transport of a novel effector protein VirE3. Nucleic Acids Res 2003; 31:860–868.

    PubMed  CAS  Google Scholar 

  122. Schrammeijer B, Risseeuw E, Pansegrau W et al. Interaction of the virulence protein VirF of Agrobacterium tumefaciens with plant homologs of the yeast Skpl protein. Curr Biol 2001; 11:258–262.

    PubMed  CAS  Google Scholar 

  123. Chook YM, Blobel G. Karyopherins and nuclear import. Curr Opin Struct Biol 2001; 11:703–715.

    PubMed  CAS  Google Scholar 

  124. Komeili A, O’Shea EK. New perspectives on nuclear transport. Annu Rev Genet 2001; 35:341–364.

    PubMed  CAS  Google Scholar 

  125. Marte B. Passage through the nuclear pore. Nat Cell Biol 2001; 3:E135.

    PubMed  CAS  Google Scholar 

  126. Quimby BB, Corbett AH. Nuclear transport mechanisms. Cell Mol Life Sci 2001; 58:1776–1773.

    Google Scholar 

  127. Hubner S, Smith HM, Hu W et al. Plant importin alpha binds nuclear localization sequences with high affinity and can mediate nuclear import independent of importin beta. J Biol Chem 1999; 274:22610–22617.

    PubMed  CAS  Google Scholar 

  128. Hicks GR, Smith HMS, Lobreaux S et al. Nuclear import in permeabilized protoplasts from higher plants has unique features. Plant Cell 1996; 8:1337–1352.

    PubMed  CAS  Google Scholar 

  129. Matsuki R, Iwasaki T, Shoji K et al. Isolation and characterization of two importin-beta genes from rice. Plant Cell Physiol 1998; 39:879–884.

    PubMed  CAS  Google Scholar 

  130. Citovsky V, Zambryski PC. Transport of nucleic acids through membrane channels: Snaking through small holes. Annu Rev Microbiol 1993; 47:167–197.

    PubMed  CAS  Google Scholar 

  131. Mehlin H, Daneholt B, Skoglund U. Translocation of a specific premessenger ribonucleoprotein particle through the nuclear pore studied with electron microscope tomography. Cell 1992; 69:605–613.

    PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Biochemistry and Cell Biology, State University of New York at Stony Brook, Stony Brook, New York, USA

    Tzvi Tzfira, Benoit Lacroix & Vitaly Citovsky

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  1. Tzvi Tzfira
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  2. Benoit Lacroix
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  3. Vitaly Citovsky
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Tzfira, T., Lacroix, B., Citovsky, V. (2005). Nuclear Import of Agrobacterium T-DNA. In: Nuclear Import and Export in Plants and Animals. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/0-387-27747-1_6

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