Open AccessThe stem rust resistance gene Rpg5 encodes a protein with nucleotide-binding-site, leucine-rich, and protein kinase domains
Author(s) -
Robert Brueggeman,
Arnis Druka,
Jayaveeramuthu Nirmala,
Tim Cavileer,
Tom Drader,
Nils Rostoks,
Aghafakhr Mirlohi,
Harvinder Bennypaul,
U. S. Gill,
David Kudrna,
C. Bruce A. Whitelaw,
Andrzej Kilian,
Feng Han,
Yujun Sun,
Kulvinder S. Gill,
Brian J. Steffenson,
A. Kleinhofs
Publication year - 2008
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0807270105
Subject(s) - biology , gene , genetics , stem rust , hspa2 , leucine rich repeat , gene silencing , microbiology and biotechnology , peptide sequence
We isolated the barley stem rust resistance genesRpg5 andrpg4 by map-based cloning. These genes are colocalized on a 70-kb genomic region that was delimited by recombination. TheRpg5 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 candidateRpg5 gene. Allele and recombinant sequencing suggested that the probablerpg4 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.