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| Subject Categories: Differentiation & Death | Plant Biology |
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| The EMBO Journal
(2002) 21, 4511–4519, doi: 10.1093/emboj/cdf453 |
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| Interaction between domains of a plant NBS−LRR protein in disease resistance-related cell death |
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| Peter Moffett, Garry Farnham, Jack Peart and David C. Baulcombe |
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The Sainsbury Laboratory, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK To whom correspondence should be addressed David C. Baulcombe, david.baulcombe@sainsbury-laboratory.ac.uk Received 14 May 2002; Revised 9 July 2002; Accepted 11 July 2002. |
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| Abstract |
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| Many plant disease resistance (R) genes encode proteins predicted to have an N-terminal coiled-coil (CC) domain, a central nucleotide-binding site (NBS) domain and a C-terminal leucine-rich repeat (LRR) domain. These CC−NBS−LRR proteins recognize specific pathogen-derived products and initiate a resistance response that often includes a type of cell death known as the hypersensitive response (HR). Co-expression of the potato CC−NBS−LRR protein Rx and its elicitor, the PVX coat protein (CP), results in a rapid HR. Surprisingly, co-expression of the LRR and CC−NBS as separate domains also resulted in a CP-dependent HR. Likewise, the CC domain complemented a version of Rx lacking this domain (NBS−LRR). Correspondingly, the LRR domain interacted physically in planta with the CC−NBS, as did CC with NBS−LRR. Both interactions were disrupted in the presence of CP. However, the interaction between CC and NBS−LRR was dependent on a wild-type P-loop motif, whereas the interaction between CC−NBS and LRR was not. We propose that activation of Rx entails sequential disruption of at least two intramolecular interactions. |
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| Keywords: disease resistance, hypersensitive response, NBS−LRR, PVX, R gene |
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