The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein
Identifieur interne : 000A43 ( Pmc/Checkpoint ); précédent : 000A42; suivant : 000A44The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein
Auteurs : Ann-Maree Catanzariti [États-Unis] ; Peter N. Dodds [Australie] ; Thomas Ve [Australie] ; Bostjan Kobe [Australie] ; Jeffrey G. Ellis [Australie] ; Brian J. Staskawicz [États-Unis]Source :
- Molecular plant-microbe interactions : MPMI [ 0894-0282 ] ; 2010.
Abstract
In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M–AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.
Url:
DOI: 10.1094/MPMI-23-1-0049
PubMed: 19958138
PubMed Central: 3142614
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="P1">In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M–AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</p>
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Department of Plant and Microbial Biology, 111 Koshland Hall, University of California, Berkeley 94720-3102, U.S.A</aff>
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Commonwealth Scientific and Industrial Research Organisation, Division of Plant Industry, GPO Box 1600, Canberra ACT 2601, Australia</aff>
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School of Chemistry and Molecular Biosciences and Institute for Molecular Bioscience, University of Queensland, Brisbane QLD 4072, Australia</aff>
<author-notes><corresp id="FN1">Corresponding author: B. J. Staskawicz; Telephone: +1 510 642 3721; Fax: +1 510 642 4995; <email>stask@berkeley.edu</email>
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<abstract><p id="P1">In plant immunity, recognition of pathogen effectors by plant resistance proteins leads to the activation of plant defenses and a localized cell death response. The AvrM effector from flax rust is a small secreted protein that is recognized by the M resistance protein in flax. Here, we investigate the mechanism of M–AvrM recognition and show that these two proteins directly interact in a yeast two-hybrid assay, and that this interaction correlates with the recognition specificity observed for each of the different AvrM variants. We further characterize this interaction by demonstrating that the C-terminal domain of AvrM is required for M-dependent cell death, and show that this domain also interacts with the M protein in yeast. We investigate the role of C-terminal differences among the different AvrM proteins for their involvement in this interaction and establish that M recognition is hindered by an additional 34 amino acids present at the C terminus of several AvrM variants. Structural characterization of recombinant AvrM-A protein revealed a globular C-terminal domain that dimerizes.</p>
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