A mutation within the leucine-rich repeat domain of the Arabidopsis disease resistance gene RPS5 partially suppresses multiple bacterial and downy mildew resistance genes.
Recognition of pathogens by plants is mediated by several distinct families of functionally variable but structurally related disease resistance (R) genes. The largest family is defined by the presence of a putative nucleotide binding domain and 12 to 21 leucine-rich repeats (LRRs). The function of these LRRs has not been defined, but they are speculated to bind pathogen-derived ligands. We have isolated a mutation in the Arabidopsis RPS5 gene that indicates that the LRR region may interact with other plant proteins. The rps5-1 mutation causes a glutamate-to-lysine substitution in the third LRR and partially compromises the function of several R genes that confer bacterial and downy mildew resistance. The third LRR is relatively well conserved, and we speculate that it may interact with a signal transduction component shared by multiple R gene pathways.
Department of Biology, Indiana University, Bloomington, Indiana 47405, USA.
R F
RF
Warren
A
A
Henk
P
P
Mowery
E
E
Holub
R W
RW
Innes
D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics* / Q000382:microbiology*; D001483:Base Sequence; D018744:DNA, Plant / Q000235:genetics; D017343:Genes, Plant; D005816:Genetic Complementation Test; D008969:Molecular Sequence Data; D005810:Multigene Family; D009154:Mutation; D009868:Oomycetes / Q000472:pathogenicity; D010935:Plant Diseases / Q000235:genetics* / Q000382:microbiology*; D030821:Plants, Genetically Modified; D011549:Pseudomonas / Q000472:pathogenicity; D020449:Repetitive Sequences, Amino Acid; D017386:Sequence Homology, Amino Acid
D018744:DNA, Plant