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Biological systems of the host cell involved in Agrobacterium infection
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Citovsky V., Kozlovsky S.V., Lacriox B., Zaltsman A., Dafny-Yelin M., Vyas S., Tovkach A., and Tzfira T. Biological systems of the host cell involved in Agrobacterium infection. Cell Microbiol 9 (2007) 9-20
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Dafny-Yelin M., Levy A., and Tzfira T. The ongoing saga of Agrobacterium-host interactions. Trends Plant Sci 13 (2008) 102-105
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Agrobacterium in the genomics age
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This recent review discusses how genomic approaches have revealed important mechanisms of Agrobacterium-mediated plant transformation.
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Gelvin S.B. Agrobacterium in the genomics age. Plant Physiol 150 (2009) 1665-1676. This recent review discusses how genomic approaches have revealed important mechanisms of Agrobacterium-mediated plant transformation.
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The Agrobacterium tumefaciens virE2 gene product is a single-stranded-DNA-binding protein that associates with T-DNA
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Cooperative interaction of Agrobacterium VirE2 protein with single-stranded DNA: implications for the T-DNA transfer process
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Association of single-stranded transferred DNA from Agrobacterium tumefaciens with tobacco cells
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Yusibov V.M., Steck T.R., Gupta V., and Gelvin S.B. Association of single-stranded transferred DNA from Agrobacterium tumefaciens with tobacco cells. Proc Natl Acad Sci U S A 91 (1994) 2994-2998
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The emerging structure of the Agrobacterium T-DNA transfer complex
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Howard E., and Citovsky V. The emerging structure of the Agrobacterium T-DNA transfer complex. BioEssays 12 (1990) 103-108
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The VirD2 pilot protein of Agrobacterium-transferred DNA interacts with the TATA box-binding protein and a nuclear protein kinase in plants
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Bakó L., Umeda M., Tiburcio A.F., Schell J., and Koncz C. 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 U S A 100 (2003) 10108-10113
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Bakó, L.1
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13
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0032499718
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Agrobacterium VirD2 protein interacts with plant host cyclophilins
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Deng W., Chen L., Wood D.W., Metcalfe T., Liang X., Gordon M.P., Comai L., and Nester E.W. Agrobacterium VirD2 protein interacts with plant host cyclophilins. Proc Natl Acad Sci U S A 95 (1998) 7040-7045
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14
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0030885876
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Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein
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Ballas N., and Citovsky V. Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein. Proc Natl Acad Sci U S A 94 (1997) 10723-10728
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Proc Natl Acad Sci U S A
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Ballas, N.1
Citovsky, V.2
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15
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54849442381
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AtImpa-4, an Arabidopsis importin α isoform, is preferentially involved in Agrobacterium-mediated plant transformation
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This paper shows the importance of a particular importin α isoform, IMPa-4, in Agrobacterium-mediated plant transformation. The paper also shows that VirE2 localizes in the plant cytoplasm except when interacting with IMPa-4, in which case the interacting proteins can enter the nucleus.
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Bhattacharjee S., Lee L.-Y., Oltmanns H., Cao H., Veena, Cuperus J., and Gelvin S.B. AtImpa-4, an Arabidopsis importin α isoform, is preferentially involved in Agrobacterium-mediated plant transformation. Plant Cell 20 (2008) 2661-2680. This paper shows the importance of a particular importin α isoform, IMPa-4, in Agrobacterium-mediated plant transformation. The paper also shows that VirE2 localizes in the plant cytoplasm except when interacting with IMPa-4, in which case the interacting proteins can enter the nucleus.
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(2008)
Plant Cell
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Bhattacharjee, S.1
Lee, L.-Y.2
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Cao, H.4
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Cuperus, J.6
Gelvin, S.B.7
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16
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1842787809
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Expression of plant protein phosphatase 2C interferes with nuclear import of the Agrobacterium T-complex protein VirD2
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Tao Y., Rao P.K., Bhattacharjee S., and Gelvin S.B. Expression of plant protein phosphatase 2C interferes with nuclear import of the Agrobacterium T-complex protein VirD2. Proc Natl Acad Sci U S A 101 (2004) 5164-5169
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Tao, Y.1
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17
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0035796396
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VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2, is involved in VirE2 nuclear import and Agrobacterium infectivity
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Tzfira T., Vaidya M., and Citovsky V. VIP1, an Arabidopsis protein that interacts with Agrobacterium VirE2, is involved in VirE2 nuclear import and Agrobacterium infectivity. EMBO J 20 (2001) 3596-3607
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Tzfira, T.1
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Citovsky, V.3
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18
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55749100859
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Association of the Agrobacterium T-DNA-protein complex with plant nucleosomes
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This paper shows that the VirE2 interacting protein VIP1 can target VirE2 and single-strand DNA to nucleosomes in vitro and, therefore, may target the T-complex to plant chromatin in vivo.
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Lacriox B., Loyter A., and Citovsky V. Association of the Agrobacterium T-DNA-protein complex with plant nucleosomes. Proc Natl Acad Sci U S A 105 (2008) 15429-15434. This paper shows that the VirE2 interacting protein VIP1 can target VirE2 and single-strand DNA to nucleosomes in vitro and, therefore, may target the T-complex to plant chromatin in vivo.
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Proc Natl Acad Sci U S A
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Lacriox, B.1
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19
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The plant VirE2 interacting protein 1. A molecular link between the Agrobacterium T-complex and the host cell chromatin?
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Loyter A., Rosenbluh J., Zakai N., Li J., Kozlovsky S.V., Tzfira T., and Citovsky V. The plant VirE2 interacting protein 1. A molecular link between the Agrobacterium T-complex and the host cell chromatin?. Plant Physiol 138 (2005) 1318-1321
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Plant Physiol
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Loyter, A.1
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Citovsky, V.7
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20
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34347382316
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Arabidopsis VirE2 Interacting Protein2 is required for Agrobacterium T-DNA integration in plants
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Anand A., Krichevsky A., Schomack S., Lahaye T., Tzfira T., Tang Y., Citovsky V., and Mysore K.S. Arabidopsis VirE2 Interacting Protein2 is required for Agrobacterium T-DNA integration in plants. Plant Cell 19 (2007) 1695-1708
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Plant Cell
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Anand, A.1
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21
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0025598893
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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
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Herrera-Estrella A., Van Montagu M., and 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 U S A 87 (1990) 9534-9537
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The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: implications for nuclear uptake of DNA in plant cells
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Howard E.A., Zupan J.R., Citovsky V., and Zambryski P.C. The VirD2 protein of A. tumefaciens contains a C-terminal bipartite nuclear localization signal: implications for nuclear uptake of DNA in plant cells. Cell 68 (1992) 109-118
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The T-DNA-linked VirD2 protein contains two distinct functional nuclear localization signals
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Tinland B., Koukolikova-Nicola Z., Hall M.N., and Hohn B. The T-DNA-linked VirD2 protein contains two distinct functional nuclear localization signals. Proc Natl Acad Sci U S A 89 (1992) 7442-7446
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The VirD2 protein of Agrobacterium tumefaciens carries nuclear localization signals important for transfer of T-DNA to plants
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Rossi L., Hohn B., and Tinland B. The VirD2 protein of Agrobacterium tumefaciens carries nuclear localization signals important for transfer of T-DNA to plants. Mol Gen Genet 239 (1993) 345-353
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Nuclear import of Agrobacterium VirD2 and VirE2 proteins in maize and tobacco
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Citovsky V., Warnick D., and Zambryski P. Nuclear import of Agrobacterium VirD2 and VirE2 proteins in maize and tobacco. Proc Natl Acad Sci U S A 91 (1994) 3210-3214
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26
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Role of the Agrobacterium tumefaciens VirD2 protein in T-DNA transfer and integration
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Mysore K.S., Bassuner B., Deng X.-B., Darbinian N.S., Motchoulski A., Ream W., and Gelvin S.B. Role of the Agrobacterium tumefaciens VirD2 protein in T-DNA transfer and integration. Mol Plant-Microbe Interact 11 (1998) 668-683
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Mysore, K.S.1
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Gelvin, S.B.7
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27
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0029864256
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Agrobacterium VirE2 protein mediates nuclear uptake of single-stranded DNA in plant cells
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Zupan J.R., Citovsky V., and Zambryski P. Agrobacterium VirE2 protein mediates nuclear uptake of single-stranded DNA in plant cells. Proc Natl Acad Sci U S A 93 (1996) 2392-2397
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0035097843
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Import of Agrobacterium T-DNA into plant nuclei: two distinct functions of VirD2 and VirE2 proteins
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Ziemienowicz A., Merkle T., Schoumacher F., Hohn B., and Rossi L. Import of Agrobacterium T-DNA into plant nuclei: two distinct functions of VirD2 and VirE2 proteins. Plant Cell 13 (2001) 369-383
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Ziemienowicz, A.1
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0034923226
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Comparison between nuclear localization of nopaline- and octopine-specific Agrobacterium VirE2 proteins in plant, yeast and mammalian cells
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Tzfira T., and Citovsky V. Comparison between nuclear localization of nopaline- and octopine-specific Agrobacterium VirE2 proteins in plant, yeast and mammalian cells. Mol Plant Pathol 2 (2001) 171-176
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Mol Plant Pathol
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Tzfira, T.1
Citovsky, V.2
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30
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40149088163
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VirE2: a unique ssDNA-compacting molecular machine
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This biophysical paper demonstrates that VirE2 interaction with single-strand DNA can compact DNA or serve as an ATP-independent force to pull DNA through a membrane. The paper also shows cytoplasmic and perhaps membrane localization of VirE2 in plant cells.
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Grange W., Duckely M., Husale S., Jacob S., Engel A., and Hegner M. VirE2: a unique ssDNA-compacting molecular machine. PLoS Biol 6 (2008) 343-351. This biophysical paper demonstrates that VirE2 interaction with single-strand DNA can compact DNA or serve as an ATP-independent force to pull DNA through a membrane. The paper also shows cytoplasmic and perhaps membrane localization of VirE2 in plant cells.
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(2008)
PLoS Biol
, vol.6
, pp. 343-351
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Grange, W.1
Duckely, M.2
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31
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54849417596
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Vectors for multi-color bimolecular fluorescence complementation to investigate protein-protein interactions in living plant cells
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Lee L.-Y., Fang M.-J., Kuang L.-Y., and Gelvin S.B. Vectors for multi-color bimolecular fluorescence complementation to investigate protein-protein interactions in living plant cells. Plant Methods 4 (2008) 24
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(2008)
Plant Methods
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Lee, L.-Y.1
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70849094968
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VIP1 response elements mediate mitogen-activated protein kinase 3-induced stress gene expression
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Pitzschke A., Djamei A., Teige M., and Hirt H. VIP1 response elements mediate mitogen-activated protein kinase 3-induced stress gene expression. Proc Natl Acad Sci U S A 106 (2009) 18414-18419
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Trojan horse strategy in Agrobacterium transformation: Abusing MAPK defense signaling
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This important paper shows that the phosphorylation of VIP1 is important for its nuclear localization and, therefore likely, nuclear localization of VirE2.
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Djamei A., Pitzschke A., Nakagami H., Rajh I., and Hirt H. Trojan horse strategy in Agrobacterium transformation: Abusing MAPK defense signaling. Science 318 (2007) 453-456. This important paper shows that the phosphorylation of VIP1 is important for its nuclear localization and, therefore likely, nuclear localization of VirE2.
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Science
, vol.318
, pp. 453-456
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Djamei, A.1
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An Agrobacterium VirE2 channel for transferred-DNA transport into plant cells
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Dumas F., Duckely M., Pelczar P., Van Gelder P., and Hohn B. An Agrobacterium VirE2 channel for transferred-DNA transport into plant cells. Proc Natl Acad Sci U S A 98 (2001) 485-490
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The VirE1VirE2 complex of Agrobacterium tumefaciens interacts with single-stranded DNA and forms channels
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Duckely M., Oomen C., Axthelm F., Van Gelder P., Waksman G., and Engel A. The VirE1VirE2 complex of Agrobacterium tumefaciens interacts with single-stranded DNA and forms channels. Mol Microbiol 58 (2005) 1130-1142
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The carboxy-terminus of VirE2 from Agrobacterium tumefaciens is required for its transport to host cells by the virB-encoded type IV transport system
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Simone M., McCullen C.A., Stahl L.E., and Binns A.N. 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 41 (2001) 1283-1293
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Vergunst A.C., Schrammeijer B., den Dulk-Ras A., de Vlaam C.M.T., Regensburg-Tuink T.J.G., and Hooykaas P.J.J. VirB/D4-dependent protein translocation from Agrobacterium into plant cells. Science 290 (2000) 979-982
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Positive charge is an important feature of the C-terminal transport signal of the VirB/D4-translocated proteins of Agrobacterium
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Vergunst A.C., van Lier M.C.M., den Dulk-Ras A., Stuve T.A.G., Ouwehand A., and Hooykaas P.J.J. Positive charge is an important feature of the C-terminal transport signal of the VirB/D4-translocated proteins of Agrobacterium. Proc Natl Acad Sci U S A 102 (2005) 832-837
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Mutagenesis of the Agrobacterium VirE2 single-stranded DNA-binding protein identifies regions required for self-association and interaction with VirE1 and a permissive site for hybrid protein construction
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Zhou X.-R., and Christie P.J. Mutagenesis of the Agrobacterium VirE2 single-stranded DNA-binding protein identifies regions required for self-association and interaction with VirE1 and a permissive site for hybrid protein construction. J Bacteriol 181 (1999) 4342-4352
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The complete nucleotide sequence of a plant root-inducing (Ri) plasmid indicates its chimeric structure and evolutionary relationship between tumor-inducing (Ti) and symbiotic (Sym) plasmids in Rhizobiaceae
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Moriguchi K., Maeda Y., Satou M., Hardayani N.S.N., Kataoka M., Tanaka N., and Yoshida K. The complete nucleotide sequence of a plant root-inducing (Ri) plasmid indicates its chimeric structure and evolutionary relationship between tumor-inducing (Ti) and symbiotic (Sym) plasmids in Rhizobiaceae. J Mol Biol 307 (2001) 771-784
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41
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49649105771
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Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners
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This paper presents important information on the structural conformation of VirE2 when bound to its chaperone VirE1. This information is useful in predicting VirE2 interacting domains with T-strands and with the nuclear shuttle proteins importin α and VIP1.
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Dym O., Albeck S., Unger T., Jacobovitch J., Branzburg A., Michael Y., Frenkiel-Krispin D., Wolf S.G., and Elbaum M. Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners. Proc Natl Acad Sci U S A 105 (2008) 11170-11175. This paper presents important information on the structural conformation of VirE2 when bound to its chaperone VirE1. This information is useful in predicting VirE2 interacting domains with T-strands and with the nuclear shuttle proteins importin α and VIP1.
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Frenkiel-Krispin, D.7
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Elbaum, M.9
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42
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VirE1 protein mediates export of the single-stranded DNA-binding protein VirE2 from Agrobacterium tumefaciens into plant cells
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Sundberg C., Meek L., Carroll K., Das A., and Ream W. VirE1 protein mediates export of the single-stranded DNA-binding protein VirE2 from Agrobacterium tumefaciens into plant cells. J Bacteriol 178 (1996) 1207-1212
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Agrobacterium rhizogenes GALLS protein substitutes for Agrobacterium tumefaciens single-stranded DNA-binding protein VirE2
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Hodges L., Cuperus J., and Ream W. Agrobacterium rhizogenes GALLS protein substitutes for Agrobacterium tumefaciens single-stranded DNA-binding protein VirE2. J Bacteriol 186 (2004) 3065-3077
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Ream, W.3
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Agrobacterium rhizogenes GALLS protein contains domains for ATP binding, nuclear localization, and type IV secretion
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Hodges L.D., Vergunst A.C., Neal-McKinney J., den Dulk-Ras A., Moyer D.M., Hooykaas P.J.J., and Ream W. Agrobacterium rhizogenes GALLS protein contains domains for ATP binding, nuclear localization, and type IV secretion. J Bacteriol 188 (2006) 8222-8230
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Hodges, L.D.1
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Moyer, D.M.5
Hooykaas, P.J.J.6
Ream, W.7
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45
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The Agrobacterium rhizogenes GALLS gene encodes two secreted proteins required for genetic transformation of plants
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Hodges L.D., Lee L.-Y., McNett H., Gelvin S.B., and Ream W. The Agrobacterium rhizogenes GALLS gene encodes two secreted proteins required for genetic transformation of plants. J Bacteriol 191 (2009) 355-364
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Ream, W.5
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46
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Agrobacterium tumefaciens and A. rhizogenes use different proteins to transport bacterial DNA into the plant cell nucleus
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This review contains interesting speculation about the roles of VirE2 and GALLS proteins in transporting VirD2/T-strands into the nucleus.
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Ream W. Agrobacterium tumefaciens and A. rhizogenes use different proteins to transport bacterial DNA into the plant cell nucleus. Micro Biotechnol 2 (2009) 416-427. This review contains interesting speculation about the roles of VirE2 and GALLS proteins in transporting VirD2/T-strands into the nucleus.
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Ream, W.1
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The VirE2 protein of Agrobacterium tumefaciens: the Yin and Yang of T-DNA transfer
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Duckely M., and Hohn B. The VirE2 protein of Agrobacterium tumefaciens: the Yin and Yang of T-DNA transfer. FEMS Microbiol Lett 223 (2003) 1-6
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