1. Chloroplastic Protein NRIP1 Mediates Innate Immune Receptor Recognition of a Viral Effector
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Caplan, Jeffrey L., Mamillapalli, Padmavathi, Burch-Smith, Tessa M., Czymmek, Kirk, and Dinesh-Kumar, S.P.
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Developmental biology ,Virus diseases ,Biological sciences - Abstract
To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/j.cell.2007.12.031 Byline: Jeffrey L. Caplan (1), Padmavathi Mamillapalli (1), Tessa M. Burch-Smith (1), Kirk Czymmek (2), S.P. Dinesh-Kumar (1) Keywords: CELLIMMUNO; MOLIMMUNO 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. Author Affiliation: (1) Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520, USA (2) Department of Biological Sciences, Delaware Biotechnology Institute, University of Delaware, Newark, DE 19711, USA Article History: Received 17 April 2007; Revised 18 October 2007; Accepted 12 December 2007 Article Note: (miscellaneous) Published: February 7, 2008
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