Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity

Wang, C., Guncar, G., Forwood, J., Teh, T., Catanzariti, A., Lawrence, G., Loughlin, F., Mackay, J., Schirra, H., Anderson, P., Ellis, J., Dodds, P. and Kobe, B. (2007) Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity. Plant Cell, 19 9: 2898-2912. doi:10.1105/tpc.107.053611


Author Wang, C.
Guncar, G.
Forwood, J.
Teh, T.
Catanzariti, A.
Lawrence, G.
Loughlin, F.
Mackay, J.
Schirra, H.
Anderson, P.
Ellis, J.
Dodds, P.
Kobe, B.
Title Crystal structures of flax rust avirulence proteins AvrL567-A and -D reveal details of the structural basis for flax disease resistance specificity
Journal name Plant Cell   Check publisher's open access policy
ISSN 1040-4651
Publication date 2007-09-14
Sub-type Article (original research)
DOI 10.1105/tpc.107.053611
Volume 19
Issue 9
Start page 2898
End page 2912
Total pages 15
Place of publication Rockville
Publisher Amer Soc Plant Biologists
Language eng
Subject C1
270103 Protein Targeting and Signal Transduction
780105 Biological sciences
Abstract The gene-for-gene mechanism of plant disease resistance involves direct or indirect recognition of pathogen avirulence (Avr) proteins by plant resistance ( R) proteins. Flax rust (Melampsora lini) AvrL567 avirulence proteins and the corresponding flax ( Linum usitatissimum) L5, L6, and L7 resistance proteins interact directly. We determined the three-dimensional structures of two members of the AvrL567 family, AvrL567-A and AvrL567-D, at 1.4- and 2.3-angstrom resolution, respectively. The structures of both proteins are very similar and reveal a beta-sandwich fold with no close known structural homologs. The polymorphic residues in the AvrL567 family map to the surface of the protein, and polymorphisms in residues associated with recognition differences for the R proteins lead to significant changes in surface chemical properties. Analysis of single amino acid substitutions in AvrL567 proteins confirm the role of individual residues in conferring differences in recognition and suggest that the specificity results from the cumulative effects of multiple amino acid contacts. The structures also provide insights into possible pathogen-associated functions of AvrL567 proteins, with nucleic acid binding activity demonstrated in vitro. Our studies provide some of the first structural information on avirulence proteins that bind directly to the corresponding resistance proteins, allowing an examination of the molecular basis of the interaction with the resistance proteins as a step toward designing new resistance specificities.
Keyword Biochemistry & Molecular Biology
Plant Sciences
Cell Biology
Leucine-rich Repeats
Pyrenophora-tritici-repentis
Pathogen Cladosporium-fulvum
For-gene Specificity
Nbs-lrr Proteins
Iii Effector
Cell-death
Ptr Toxa
Macromolecular Structures
Hypersensitive Response
Q-Index Code C1
Q-Index Status Confirmed Code

 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 70 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 75 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Tue, 19 Feb 2008, 01:29:36 EST