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Plant physiology (source)
Castelló, M.J., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain, Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Carrasco, J.L., Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Navarrete-Gómez, M., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain, Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Daniel, J., Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Granot, D., Department of Vegetable Research, Institute of Plant Sciences, Agricultural Research Organization, The Volcani Center, Bet-Dagan 50250, Israel
Vera, P., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain
DNA-binding protein phosphatases (DBPs) have been identified as a novel class of plant-specific regulatory factors playing aírole in plant-virus interactions. NtDBP1 from tobacco (Nicotiana tabacum) was shown to participate in transcriptional regulationíof gene expression in response to virus infection in compatible interactions, and AtDBP1, its closest relative in the model plantíArabidopsis (Arabidopsis thaliana), has recently been found to mediate susceptibility to potyvirus, one of the most speciose taxaíof plant viruses. Here, we report on the identification of a novel family of highly conserved small polypeptides that interactíwith DBP1 proteins both in tobacco and Arabidopsis, which we have designated DBP-interacting protein 2 (DIP2). Theíinteraction of AtDIP2 with AtDBP1 was demonstrated in vivo by bimolecular fluorescence complementation, and AtDIP2 wasíshown to functionally interfere with AtDBP1 in yeast. Furthermore, reducing AtDIP2 gene expression leads to increasedísusceptibility to the potyvirus Plum pox virus and to a lesser extent also to Turnip mosaic virus, whereas overexpression results iníenhanced resistance. Therefore, we describe a novel family of conserved small polypeptides in plants and identify AtDIP2 as aínovel host factor contributing to resistance to potyvirus in Arabidopsis. © 2011 American Society of Plant Biologists. All Rights Reserved.
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A plant small polypeptide is a novel component of DNA-binding protein phosphatase 1-mediated resistance to Plum pox virus in Arabidopsis
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Castelló, M.J., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain, Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Carrasco, J.L., Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Navarrete-Gómez, M., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain, Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Daniel, J., Centre de Genetique Moleculaire, Centre National de la Recherche Scientifique, 91198 Gif-sur-Yvette, France
Granot, D., Department of Vegetable Research, Institute of Plant Sciences, Agricultural Research Organization, The Volcani Center, Bet-Dagan 50250, Israel
Vera, P., Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain
A plant small polypeptide is a novel component of DNA-binding protein phosphatase 1-mediated resistance to Plum pox virus in Arabidopsis
DNA-binding protein phosphatases (DBPs) have been identified as a novel class of plant-specific regulatory factors playing aírole in plant-virus interactions. NtDBP1 from tobacco (Nicotiana tabacum) was shown to participate in transcriptional regulationíof gene expression in response to virus infection in compatible interactions, and AtDBP1, its closest relative in the model plantíArabidopsis (Arabidopsis thaliana), has recently been found to mediate susceptibility to potyvirus, one of the most speciose taxaíof plant viruses. Here, we report on the identification of a novel family of highly conserved small polypeptides that interactíwith DBP1 proteins both in tobacco and Arabidopsis, which we have designated DBP-interacting protein 2 (DIP2). Theíinteraction of AtDIP2 with AtDBP1 was demonstrated in vivo by bimolecular fluorescence complementation, and AtDIP2 wasíshown to functionally interfere with AtDBP1 in yeast. Furthermore, reducing AtDIP2 gene expression leads to increasedísusceptibility to the potyvirus Plum pox virus and to a lesser extent also to Turnip mosaic virus, whereas overexpression results iníenhanced resistance. Therefore, we describe a novel family of conserved small polypeptides in plants and identify AtDIP2 as aínovel host factor contributing to resistance to potyvirus in Arabidopsis. © 2011 American Society of Plant Biologists. All Rights Reserved.
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