Abstract
Plant innate immunity relies on the recognition of pathogen effector molecules by nucleotide-binding-leucine-rich repeat (NB-LRR) immune receptor families. Previously we have shown the N immune receptor, a member of TIR-NB-LRR family, indirectly recognizes the 50 kDa helicase (p50) domain of Tobacco mosaic virus (TMV) through its TIR domain. We have identified an N receptor-interacting protein, NRIP1, that directly interacts with both N's TIR domain and p50. NRIP1 is a functional rhodanese sulfurtransferase and is required for N to provide complete resistance to TMV. Interestingly, NRIP1 that normally localizes to the chloroplasts is recruited to the cytoplasm and nucleus by the p50 effector. As a consequence, NRIP1 interacts with N only in the presence of the p50 effector. Our findings show that a chloroplastic protein is intimately involved in pathogen recognition. We propose that N's activation requires a prerecognition complex containing the p50 effector and NRIP1.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Adaptor Proteins, Signal Transducing / analysis
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Adaptor Proteins, Signal Transducing / immunology*
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Adaptor Proteins, Signal Transducing / metabolism
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Antigens, Viral / immunology
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Cell Nucleus / chemistry
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Chloroplasts / chemistry
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Cytoplasm / chemistry
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Immunity, Innate
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Nicotiana / immunology*
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Nicotiana / virology
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Nuclear Proteins / analysis
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Nuclear Proteins / immunology*
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Nuclear Proteins / metabolism
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Nuclear Receptor Interacting Protein 1
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Plant Diseases / immunology*
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Plant Proteins / analysis
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Plant Proteins / immunology*
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Plant Proteins / metabolism
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Protein Structure, Tertiary
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Receptors, Virus / analysis
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Receptors, Virus / immunology*
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Receptors, Virus / metabolism
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Thiosulfate Sulfurtransferase / metabolism
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Tobacco Mosaic Virus / immunology*
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Two-Hybrid System Techniques
Substances
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Adaptor Proteins, Signal Transducing
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Antigens, Viral
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Nuclear Proteins
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Nuclear Receptor Interacting Protein 1
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Plant Proteins
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Receptors, Virus
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Thiosulfate Sulfurtransferase