The stem rust resistance gene Rpg5 encodes a protein with nucleotide-binding-site, leucine-rich, and protein kinase domains

• DOI: 10.1073/pnas.0807270105
• Publication Date: 2008-09-24T01:27:34Z
• Authors: R. Brueggeman; A. Druka; J. Nirmala; T. Cavileer; T. Drader; N. Rostoks; A. Mirlohi; H. Bennypaul; U. Gill; D. Kudrna; C. Whitelaw; A. Kilian; F. Han; Y. Sun; K. Gill; B. Steffenson; A. Kleinhofs
• Keywords: 0301 basic medicine; 0303 health sciences; Binding Sites; Plant Stems; Nucleotides; map-based cloning; Fungi; Hordeum; Genes, Plant; Physical Chromosome Mapping; Protein Structure, Tertiary; 03 medical and health sciences; Leucine; actin depolymerizing factor; Pg f. sp. tritici; disease resistance domains; Gene Silencing; Cloning, Molecular; Puccinia graminis; Protein Kinases; Plant Diseases; Plant Proteins

We isolated the barley stem rust resistance genes Rpg5 and rpg4 by map-based cloning. These genes are colocalized on a 70-kb genomic region that was delimited by recombination. The Rpg5 gene consists of an unusual structure encoding three typical plant disease resistance protein domains: nucleotide-binding site, leucine-rich repeat, and serine threonine protein kinase. The predicted RPG5 protein has two putative transmembrane sites possibly involved in membrane binding. The gene is expressed at low but detectable levels. Posttranscriptional gene silencing using VIGS resulted in a compatible reaction with a normally incompatible stem rust pathogen. Allele sequencing also validated the candidate Rpg5 gene. Allele and recombinant sequencing suggested that the probable rpg4 gene encoded an actin depolymerizing factor-like protein. Involvement of actin depolymerizing factor genes in nonhost resistance has been documented, but discovery of their role in gene-for-gene interaction would be novel and needs to be further substantiated.