ArticleThe Plant cell2008
IMPa-4, an Arabidopsis importin alpha isoform, is preferentially involved in agrobacterium-mediated plant transformation.
Article in The Plant cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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66 citing papers in PubMed, 123 citations in OpenAlex.
- Arabidopsis DNA repair mutants can integrate Agrobacterium T-DNA into the plant genome.The New phytologist · 2026Article
- Myosin VIII and XI isoforms interact with the Agrobacterium VirE2 protein and facilitate its transport from the plasma membrane to the perinuclear region during plant transformation.Plant communications · 2026Article
- Cas9-mediated gene-editing frequency in microalgae is doubled by harnessing the interaction between importin α and phytopathogenic NLSs.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Genomic consequences associated with Agrobacterium-mediated transformation of plants.The Plant journal : for cell and molecular biology · 2024Review
- Proteome and Interactome Linked to Metabolism, Genetic Information Processing, and Abiotic Stress in Gametophytes of Two Woodferns.International journal of molecular sciences · 2023Article
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- A nuclear import pathway exploited by pathogenic noncoding RNAs.The Plant cell · 2022Article
- OsWRKY62 and OsWRKY76 Interact with Importin α1s for Negative Regulation of Defensive Responses in Rice Nucleus.Rice (New York, N.Y.) · 2022Article
- Increased Agrobacterium-mediated transformation of Saccharomyces cerevisiae after deletion of the yeast ADA2 gene.Letters in applied microbiology · 2022Article
- An Arabidopsis nonhost resistance gene,Current research in microbial sciences · 2022Article
- Genetic factors governing bacterial virulence and host plant susceptibility duringAdvances in genetics · 2022Review
- SWO1 modulates cell wall integrity under salt stress by interacting with importin ɑ in Arabidopsis.Stress biology · 2021Article
- Nucleocytoplasmic Communication in Healthy and Diseased Plant Tissues.Frontiers in plant science · 2021Review
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- Identification and Characterization of Plant-Interacting Targets of Tomato Spotted Wilt Virus Silencing Suppressor.Pathogens (Basel, Switzerland) · 2021Article
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- Nuclear import of LIKE HETEROCHROMATIN PROTEIN1 is redundantly mediated by importins α-1, α-2 and α-3.The Plant journal : for cell and molecular biology · 2020Article
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- Review
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6 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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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