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 a role in plant-virus interactions. NtDBP1 from tobacco (Nicotiana tabacum) was shown to participate in transcriptional regulation of gene expression in response to virus infection in compatible interactions, and AtDBP1, its closest relative in the model plant Arabidopsis (Arabidopsis thaliana), has recently been found to mediate susceptibility to potyvirus, one of the most speciose taxa of plant viruses. Here, we report on the identification of a novel family of highly conserved small polypeptides that interact with DBP1 proteins both in tobacco and Arabidopsis, which we have designated DBP-interacting protein 2 (DIP2). The interaction of AtDIP2 with AtDBP1 was demonstrated in vivo by bimolecular fluorescence complementation, and AtDIP2 was shown to functionally interfere with AtDBP1 in yeast. Furthermore, reducing AtDIP2 gene expression leads to increased susceptibility to the potyvirus Plum pox virus and to a lesser extent also to Turnip mosaic virus, whereas overexpression results in enhanced resistance. Therefore, we describe a novel family of conserved small polypeptides in plants and identify AtDIP2 as a novel host factor contributing to resistance to potyvirus in Arabidopsis.
Instituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain.
María José
MJ
Castelló
Jose Luis
JL
Carrasco
Marisa
M
Navarrete-Gómez
Jacques
J
Daniel
David
D
Granot
Pablo
P
Vera
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000378:metabolism* / Q000821:virology; D029681:Arabidopsis Proteins / Q000235:genetics / Q000378:metabolism; D001483:Base Sequence; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D054884:Host-Pathogen Interactions; D008969:Molecular Sequence Data; D010455:Peptides / Q000235:genetics / Q000378:metabolism; D010749:Phosphoprotein Phosphatases / Q000235:genetics / Q000378:metabolism; D010935:Plant Diseases / Q000276:immunology* / Q000821:virology; D057865:Plant Immunity; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017801:Plum Pox Virus / Q000502:physiology*; D017800:Potyvirus / Q000502:physiology; D025941:Protein Interaction Mapping; D054645:Protein Phosphatase 1 / Q000235:genetics / Q000378:metabolism; D011993:Recombinant Fusion Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D014026:Nicotiana / Q000235:genetics* / Q000378:metabolism* / Q000821:virology; D020798:Two-Hybrid System Techniques
D029681:Arabidopsis Proteins; D004268:DNA-Binding Proteins; D010455:Peptides; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; C000592774:DBP1 protein, Arabidopsis; D010749:Phosphoprotein Phosphatases; D054645:Protein Phosphatase 1