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      The Arabidopsis downy mildew resistance gene RPP5 shares similarity to the toll and interleukin-1 receptors with N and L6.

      The Plant cell
      Alleles, Amino Acid Sequence, Animals, Arabidopsis, genetics, immunology, Arabidopsis Proteins, Base Sequence, Chromosome Mapping, DNA, Plant, chemistry, isolation & purification, Drosophila, Drosophila Proteins, Fungi, pathogenicity, Genes, Plant, Immunity, Innate, Insect Proteins, Membrane Glycoproteins, Molecular Sequence Data, Nucleic Acid Hybridization, Plant Diseases, Plant Proteins, Protein Structure, Secondary, Receptors, Cell Surface, Receptors, Interleukin-1, Sequence Alignment, Toll-Like Receptors

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          Abstract

          Plant disease resistance genes operate at the earliest steps of pathogen perception. The Arabidopsis RPP5 gene specifying resistance to the downy mildew pathogen Peronospora parasitica was positionally cloned. It encodes a protein that possesses a putative nucleotide binding site and leucine-rich repeats, and its product exhibits striking structural similarity to the plant resistance gene products N and L6. Like N and L6, the RPP5 N-terminal domain resembles the cytoplasmic domains of the Drosophila Toll and mammalian interleukin-1 transmembrane receptors. In contrast to N and L6, which produce predicted truncated products by alternative splicing, RPP5 appears to express only a single transcript corresponding to the full-length protein. However, a truncated form structurally similar to those of N and L6 is encoded by one or more other members of the RPP5 gene family that are tightly clustered on chromosome 4. The organization of repeated units within the leucine-rich repeats encoded by the wild-type RPP5 gene and an RPP5 mutant allele provides molecular evidence for the heightened capacity of this domain to evolve novel configurations and potentially new disease resistance specificities.

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