You are not currently logged in.
Access your personal account or get JSTOR access through your library or other institution:
If You Use a Screen ReaderThis content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
The Stem Rust Resistance Gene Rpg5 Encodes a Protein with Nucleotide-Binding-Site, Leucine-Rich, and Protein Kinase Domains
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 and A. Kleinhofs
Proceedings of the National Academy of Sciences of the United States of America
Vol. 105, No. 39 (Sep. 30, 2008), pp. 14970-14975
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/25464345
Page Count: 6
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Preview not available
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.
Proceedings of the National Academy of Sciences of the United States of America © 2008 National Academy of Sciences