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JXB Advance Access published online on September 19, 2005

Journal of Experimental Botany, doi:10.1093/jxb/eri288
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org
Received March 31, 2005
Accepted August 12, 2005

RESEARCH PAPER

The products of the broken Tm-2 and the durable Tm-22 resistance genes from tomato differ in four amino acids

Frank C. Lanfermeijer 1*, Jan Warmink 1, and Jacques Hille 1

1 Department Molecular Biology of Plants, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN, Haren, The Netherlands

* To whom correspondence should be addressed.
Frank C. Lanfermeijer, E-mail: f.c.lanfermeijer{at}rug.nl


   Abstract

To gain an insight into the processes underlying disease resistance and its durability, the durable Tm-22 resistance gene was compared with the broken Tm-2 resistance gene. The Tm-2 gene of tomato could be isolated via PCR with primers based on the Tm-22 sequence. The Tm-2 gene, like the Tm-22 gene, encodes an 861 amino acid polypeptide, which belongs to the coiled coil/nucleotide binding site/leucine-rich repeat class of resistance proteins. The functionality and the nature of the isolated Tm-2 gene were confirmed by introducing the gene under the control of the 35S promoter into tomato mosaic virus-susceptible tobacco. This transgenic tobacco was crossed with transgenic tobacco plants producing the movement protein (MP)-authenticated MP as the Avr protein of the Tm-2 resistance. The Tm-22 and Tm-2 open reading frames only differ in seven nucleotides, which on a protein level results in four amino acid differences, of which two are located in the nucleotide binding site and two are located in the leucine-rich repeat domain. The small difference between the two proteins suggests a highly similar interaction of these proteins with the MP, which has major implications for the concept of durability. Comparison of the two resistance-conferring alleles (Tm-2 and Tm-22) with two susceptible alleles (tm-2 and lptm-2) allowed discussion of the structure-function relationship in the Tm-2 proteins. It is proposed that the Tm-2 proteins display a partitioning of the leucine-rich repeat domain, in which the N-terminal and C-terminal parts function in signal transduction and MP recognition, respectively.

Keywords: Lycopersicon esculentum; Lycopersicon peruvianum; Tm-2; Tm-22; tomato mosaic virus; plant disease resistance gene; durability; structure-function relationships.
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