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20231227123541.0 |
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231223s2005 xx ||||| 00| ||eng c |
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|a pubmed24n1221.xml
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|a (DE-627)NLM157856437
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|a (NLM)16172136
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
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|a Lanfermeijer, Frank C
|e verfasserin
|4 aut
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| 245 |
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|a The products of the broken Tm-2 and the durable Tm-2(2) resistance genes from tomato differ in four amino acids
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|c 2005
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 10.01.2006
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|a Date Revised 13.12.2023
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a 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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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a Plant Proteins
|2 NLM
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1 |
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|a Warmink, Jan
|e verfasserin
|4 aut
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| 700 |
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|a Hille, Jacques
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 56(2005), 421 vom: 25. Nov., Seite 2925-33
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g volume:56
|g year:2005
|g number:421
|g day:25
|g month:11
|g pages:2925-33
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_ILN_350
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|a AR
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|d 56
|j 2005
|e 421
|b 25
|c 11
|h 2925-33
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