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Plant Cell Advance Online Publication
Published on December 30, 2005; 10.1105/tpc.105.037234

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Received August 19, 2005
Returned for revision November 15, 2005
Accepted December 1, 2005

Elicitor-Mediated Oligomerization of the Tobacco N Disease Resistance Protein

Pere Mestre 1 and David C. Baulcombe 1*

1 Sainsbury Laboratory, John Innes Centre, Norwich NR4 7UH, United Kingdom

* To whom correspondence should be addressed. E-mail: david.baulcombe{at}sainsbury-laboratory.ac.uk.

Plant nucleotide binding site-leucine-rich repeat (NBS-LRR) proteins are similar to the nucleotide binding oligomerization domain (NOD) protein family in their domain structure. It has been suggested that most NOD proteins rely on ligand-mediated oligomerization for function, and we have tested this possibility with the N protein of tobacco (Nicotiana tabacum). The N gene for resistance to Tobacco mosaic virus (TMV) is a member of the Toll-interleukin receptor (TIR)-NBS-LRR class of plant disease resistance (R) genes that recognizes the helicase domain from the TMV replicase. Using transient expression followed by immunoprecipitation, we show that the N protein oligomerizes in the presence of the elicitor. The oligomerization was not affected by silencing Nicotiana benthamiana ENHANCED DISEASE SUSCEPTIBILITY1 and N REQUIREMENT GENE1 cofactors of N-mediated resistance, but it was abolished by a mutation in the P-loop motif. However, loss-of-function mutations in the RNBS-A motif and in the TIR domain retain the ability to oligomerize. From these results, we conclude that oligomerization is an early event in the N-mediated resistance to TMV.






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