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Plant Cell, Vol. 13, 163-178, January 2001, Copyright © 2001, American Society of Plant Physiologists

Six Amino Acid Changes Confined to the Leucine-Rich Repeat ß-Strand/ß-Turn Motif Determine the Difference between the P and P2 Rust Resistance Specificities in Flax

Peter N. Doddsa, Gregory J. Lawrencea, and Jeffrey G. Ellisa
a Commonwealth Scientific and Industrial Research Organisation, Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia

Correspondence to: Jeffrey G. Ellis, ellisj{at}pi.csiro.au (E-mail), 61-2-6246-5000 (fax)

At least six rust resistance specificities (P and P1 to P5) map to the complex P locus in flax. The P2 resistance gene was identified by transposon tagging and transgenic expression. P2 is a member of a small multigene family and encodes a protein with nucleotide binding site (NBS) and leucine-rich repeat (LRR) domains and an N-terminal Toll/interleukin-1 receptor (TIR) homology domain, as well as a C-terminal non-LRR (CNL) domain of ~150 amino acids. A related CNL domain was detected in almost half of the predicted Arabidopsis TIR-NBS-LRR sequences, including the RPS4 and RPP1 resistance proteins, and in the tobacco N protein, but not in the flax L and M proteins. Presence or absence of this domain defines two subclasses of TIR-NBS-LRR resistance genes. Truncations of the P2 CNL domain cause loss of function, and evidence for diversifying selection was detected in this domain, suggesting a possible role in specificity determination. A spontaneous rust-susceptible mutant of P2 contained a G->E amino acid substitution in the GLPL motif, which is conserved in the NBS domains of plant resistance proteins and the animal cell death control proteins APAF-1 and CED4, providing direct evidence for the importance of this motif in resistance gene function. A P2 homologous gene isolated from a flax line expressing the P resistance specificity encodes a protein with only 10 amino acid differences from the P2 protein. Chimeric gene constructs indicate that just six of these amino acid changes, all located within the predicted ß-strand/ß-turn motif of four LRR units, are sufficient to alter P2 to the P specificity.




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