OPEN ACCESS ARTICLE

This Article Free via Open Access: OA OA Full Text Full Text (PDF) Supplemental Data OA All Versions of this Article: 18/2/491    most recent tpc.105.037234v1 Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via ISI Web of Science (25) Citing Articles via Google Scholar Google Scholar Articles by Mestre, P. Articles by Baulcombe, D. C. Search for Related Content PubMed PubMed Citation Articles by Mestre, P. Articles by Baulcombe, D. C. Agricola Articles by Mestre, P. Articles by Baulcombe, D. C.

Elicitor-Mediated Oligomerization of the Tobacco N Disease Resistance Protein^[W],[OA]

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

² To whom correspondence should be addressed. E-mail david.baulcombe{at}sainsbury-laboratory.ac.uk; fax 44-1603-450011.

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.

This article has been cited by other articles:

				G. J. Rairdan, S. M. Collier, M. A. Sacco, T. T. Baldwin, T. Boettrich, and P. Moffett The Coiled-Coil and Nucleotide Binding Domains of the Potato Rx Disease Resistance Protein Function in Pathogen Recognition and Signaling PLANT CELL, March 1, 2008; 20(3): 739 - 751. [Abstract] [Full Text] [PDF]

				H. A. van den Burg, D. I. Tsitsigiannis, O. Rowland, J. Lo, G. Rallapalli, D. MacLean, F. L.W. Takken, and J. D.G. Jones The F-Box Protein ACRE189/ACIF1 Regulates Cell Death and Defense Responses Activated during Pathogen Recognition in Tobacco and Tomato PLANT CELL, March 1, 2008; 20(3): 697 - 719. [Abstract] [Full Text] [PDF]

				W. I.L. Tameling and D. C. Baulcombe Physical Association of the NB-LRR Resistance Protein Rx with a Ran GTPase-Activating Protein Is Required for Extreme Resistance to Potato virus X PLANT CELL, May 1, 2007; 19(5): 1682 - 1694. [Abstract] [Full Text] [PDF]

				J. Ade, B. J. DeYoung, C. Golstein, and R. W. Innes Indirect activation of a plant nucleotide binding site-leucine-rich repeat protein by a bacterial protease PNAS, February 13, 2007; 104(7): 2531 - 2536. [Abstract] [Full Text] [PDF]

				W. I.L. Tameling, J. H. Vossen, M. Albrecht, T. Lengauer, J. A. Berden, M. A. Haring, B. J.C. Cornelissen, and F. L.W. Takken Mutations in the NB-ARC Domain of I-2 That Impair ATP Hydrolysis Cause Autoactivation Plant Physiology, April 1, 2006; 140(4): 1233 - 1245. [Abstract] [Full Text] [PDF]