The products of the broken Tm-2 and the durable Tm-2(2) resistance genes from tomato differ in four amino acids
To gain an insight into the processes underlying disease resistance and its durability, the durable Tm-2(2) 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-2(2) sequence. The Tm-2 gene, like the Tm-2(2)...
| Veröffentlicht in: | Journal of experimental botany. - 1985. - 56(2005), 421 vom: 25. Nov., Seite 2925-33 |
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| Weitere Verfasser: | , |
| Format: | Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2005
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| Zugriff auf das übergeordnete Werk: | Journal of experimental botany |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Plant Proteins |
| Zusammenfassung: | To gain an insight into the processes underlying disease resistance and its durability, the durable Tm-2(2) 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-2(2) sequence. The Tm-2 gene, like the Tm-2(2) 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-2(2) 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-2(2)) 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 |
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| Beschreibung: | Date Completed 10.01.2006 Date Revised 13.12.2023 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1460-2431 |