1999
DOI: 10.2307/3870876
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Identification of Regions in Alleles of the Flax Rust Resistance Gene L That Determine Differences in Gene-for-Gene Specificity

Abstract: Thirteen alleles (L, L1 to L11, and LH) from the flax L locus, which encode Toll/interleukin-1 receptor homology-nucleotide binding site-leucine-rich repeat (TIR-NBS-LRR) rust resistance proteins, were sequenced and compared to provide insight into their evolution and into the determinants of gene-for-gene resistance specificity. The predicted L6 and L11 proteins differ solely in the LRR region, whereas L6 and L7 differ solely in the TIR region. Thus, specificity differences between alleles can be determined b… Show more

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Cited by 121 publications
(209 citation statements)
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“…Many of the structural and sequence differences among the L alleles are confined to the LRR coding region, indicating involvement of the LRR domain in ligand specificity 36 . Additionally, substitution of the L2 LRR domain for the LRR domain of the L6 or L10 isoform results in L2 pathogen specificity 36 . However, some alleles with different pathogen specificity contain identical LRR domains, suggesting that sequences outside the LRR domain influence ligand specificity.…”
Section: The Lrr As An Effector-binding Domainmentioning
confidence: 99%
See 1 more Smart Citation
“…Many of the structural and sequence differences among the L alleles are confined to the LRR coding region, indicating involvement of the LRR domain in ligand specificity 36 . Additionally, substitution of the L2 LRR domain for the LRR domain of the L6 or L10 isoform results in L2 pathogen specificity 36 . However, some alleles with different pathogen specificity contain identical LRR domains, suggesting that sequences outside the LRR domain influence ligand specificity.…”
Section: The Lrr As An Effector-binding Domainmentioning
confidence: 99%
“…However, some alleles with different pathogen specificity contain identical LRR domains, suggesting that sequences outside the LRR domain influence ligand specificity. Likewise, some chimeric L molecules have demonstrated previously unknown specificities, also suggesting that multiple domains contribute to pathogen-recognition specificity 36,37 .…”
Section: The Lrr As An Effector-binding Domainmentioning
confidence: 99%
“…In each LRR, a region of the consensus sequence (xxLxLxx) is predicted to form a ␀-strand/ ␀-turn structure in which the variable residues (x) are exposed to the solvent and determine the specificity of the interaction. This region of the LRR is subjected to diversifying selection in plant resistance genes (McDowell et al, 1998;Meyers et al, 1998;Ellis et al, 1999;Van der Hoorn et al, 2001). The observation that among different LRXs, the solvent-exposed amino acids are well conserved or even identical (AtLRX3/4 and AtLRX6/7) suggests that the LRX proteins interact with very similar or identical ligands.…”
mentioning
confidence: 99%
“…De fato, em vĂĄrios sistemas planta-patĂłgeno, a variação da sequĂȘncia na regiĂŁo LRR tem mostrado ser responsĂĄvel por diferentes especificidades de reconhecimento ou de resistĂȘncia Thomas et al, 1997;Botella et al, 1998;Wang et al, 1998;Ellis et al, 1999).…”
Section: Resultsunclassified