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Plant Cell Advance Online Publication
Published on October 3, 2008; 10.1105/tpc.108.060467

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Received May 9, 2008
Returned for revision August 15, 2008
Accepted September 15, 2008

IMPa-4, an Arabidopsis Importin {alpha} Isoform, Is Preferentially Involved in Agrobacterium-Mediated Plant Transformation

Saikat Bhattacharjee 1, Lan-Ying Lee 1, Heiko Oltmanns 1, Hongbin Cao 1, Veena 1, Joshua Cuperus 1, and Stanton B. Gelvin 1*

1 Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907

* To whom correspondence should be addressed. E-mail: gelvin{at}bilbo.bio.purdue.edu.

Successful transformation of plants by Agrobacterium tumefaciens requires that the bacterial T-complex actively escorts T-DNA into the host’s nucleus. VirD2 and VirE2 are virulence proteins on the T-complex that have plant-functional nuclear localization signal sequences that may recruit importin {alpha} proteins of the plant for nuclear import. In this study, we evaluated the involvement of seven of the nine members of the Arabidopsis thaliana importin {alpha} family in Agrobacterium transformation. Yeast two-hybrid, plant bimolecular fluorescence complementation, and in vitro protein–protein interaction assays demonstrated that all tested Arabidopsis importin {alpha} members can interact with VirD2 and VirE2. However, only disruption of the importin IMPa-4 inhibited transformation and produced the rat (resistant to Agrobacterium transformation) phenotype. Overexpression of six importin {alpha} members, including IMPa-4, rescued the rat phenotype in the impa-4 mutant background. Roots of wild-type and impa-4 Arabidopsis plants expressing yellow fluorescent protein–VirD2 displayed nuclear localization of the fusion protein, indicating that nuclear import of VirD2 is not affected in the impa-4 mutant. Somewhat surprisingly, VirE2–yellow fluorescent protein mainly localized to the cytoplasm of both wild-type and impa-4 Arabidopsis cells and to the cytoplasm of wild-type tobacco (Nicotiana tabacum) cells. However, bimolecular fluorescence complementation assays indicated that VirE2 could localize to the nucleus when IMPa-4, but not when IMPa-1, was overexpressed.




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