Nuclear localization signal binding protein from
            <i>Arabidopsis</i>
            mediates nuclear import of
            <i>Agrobacterium</i>
            VirD2 protein

Ballas, Nurit; Citovsky, Vitaly

doi:10.1073/pnas.94.20.10723

Cited by 173 publications

(159 citation statements)

References 45 publications

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“…The isolation of one such putative factor recently has been reported. Ballas and Citovsky (4) showed that a plant karyopherin ␣ (AtKAP␣) can interact with VirD2 nuclear localization sequences (NLS) in a yeast two-hybrid interaction system and presumably is involved in nuclear translocation of the T-complex. Using a similar approach, a tomato type 2C protein phosphatase, DIG3, that can interact with the VirD2 NLS was identified (Y. Tao, P. Rao, and S.B.G., unpublished work).…”

Section: Discussionmentioning

confidence: 99%

An Arabidopsis histone H2A mutant is deficient in Agrobacterium T-DNA integration

Mysore

Nam

Gelvin

2000

Proc. Natl. Acad. Sci. U.S.A.

155

150

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Agrobacterium tumefaciens genetically transforms plant cells by transferring a portion of the bacterial Ti-plasmid, the T-DNA, to the plant and integrating the T-DNA into the plant genome. Little is known about the T-DNA integration process, and no plant genes involved in integration have yet been identified. We characterized an Arabidopsis mutant generated by T-DNA insertional mutagenesis, rat5, that is resistant to Agrobacterium root transformation. rat5 contains two copies of T-DNA integrated as a tandem direct repeat into the 3 untranslated region of a histone H2A gene, upstream of the polyadenylation signal sequence. Transient and stable ␤-glucuronidase expression data and assessment of the amount of T-DNA integrated into the genomes of wild-type and rat5 Arabidopsis plants indicated that the rat5 mutant is deficient in T-DNA integration. We complemented the rat5 mutation by expressing the RAT5 histone H2A gene in the mutant plant. Overexpression of RAT5 in wild-type plants increased Agrobacterium transformation efficiency. Furthermore, transient expression of a RAT5 gene from the incoming T-DNA was sufficient to complement the rat5 mutant and to increase the transformation efficiency of wild-type Arabidopsis plants.T-DNA transformation ͉ haplo-insufficiency

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Section: Discussionmentioning

confidence: 99%

An Arabidopsis histone H2A mutant is deficient in Agrobacterium T-DNA integration

Mysore

Nam

Gelvin

2000

Proc. Natl. Acad. Sci. U.S.A.

155

150

View full text Add to dashboard Cite

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“…VirD2 was exploited in yeast two-hybrid analysis to identify an Arabidopsis protein of the karyopherin-a family (AtKAPa) (Ballas and Citovsky, 1997). AtKAPa rescued a yeast mutant defective in nuclear import and mediated nuclear import of VirD2 in permeabilized yeast cells.…”

Section: Plant Nuclear Localization Signals (Table 1 Item 10)mentioning

confidence: 99%

The transfer of DNA from Agrobacterium tumefaciens into plants: a feast of fundamental insights

et al. 2000

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This review is dedicated to Jeff Schell, one of the founders of modern`Agrobiology', the genetic and molecular dissection of crown gall disease. Together with notable scientists at the University of Gent, Belgium, Jeff spearheaded the discovery of the Ti-plasmid. The elusive`tumor inducing principle' was uncloaked and provided impetus for an incredibly fruitful subsequent 25 years of analyses. Scientists all over the world were caught up in unraveling the underlying mechanisms of Agrobacterium-mediated gene transfer to plants, and along the way uncovered a movable feast of fundamental insights. Below we summarize a sampling of Agrobacterium's most recently recognized accomplishments.

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“…VirD2 promotes nuclear import through its interaction with a host karyopherin ␣ receptor (28). It also appears to be involved in intranuclear transport and in tDNA integration (29 -32).…”

mentioning

confidence: 99%

Three-dimensional Reconstruction of Agrobacterium VirE2 Protein with Single-stranded DNA

Abu‐Arish

Frenkiel-Krispin

Fricke

et al. 2004

Journal of Biological Chemistry

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Agrobacterium tumefaciens infects plant cells by a unique mechanism involving an interkingdom genetic transfer. A single-stranded DNA substrate is transported across the two cell walls along with the bacterial virulence proteins VirD2 and VirE2. A single VirD2 molecule covalently binds to the 5 -end of the singlestranded DNA, while the VirE2 protein binds stoichiometrically along the length of the DNA, without sequence specificity. An earlier transmission/scanning transmission electron microscopy study indicated a solenoidal ("telephone coil") organization of the VirE2-DNA complex. Here we report a three-dimensional reconstruction of this complex using electron microscopy and single-particle image-processing methods. We find a hollow helical structure of 15.7-nm outer diameter, with a helical rise of 51.5 nm and 4.25 VirE2 proteins/turn. The inner face of the protein units contains a continuous wall and an inward protruding shelf. These structures appear to accommodate the DNA binding. Such a quaternary arrangement naturally sequesters the DNA from cytoplasmic nucleases and suggests a mechanism for its nuclear import by decoration with host cell factors. Coexisting with the helices, we also found VirE2 tetrameric ring structures. A two-dimensional average of the latter confirms the major features of the threedimensional reconstruction.

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Nuclear localization signal binding protein from Arabidopsis mediates nuclear import of Agrobacterium VirD2 protein

Cited by 173 publications

References 45 publications

An Arabidopsis histone H2A mutant is deficient in Agrobacterium T-DNA integration

An Arabidopsis histone H2A mutant is deficient in Agrobacterium T-DNA integration

The transfer of DNA from Agrobacterium tumefaciens into plants: a feast of fundamental insights

Three-dimensional Reconstruction of Agrobacterium VirE2 Protein with Single-stranded DNA

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