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The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein

Identifieur interne : 000189 ( Ncbi/Checkpoint ); précédent : 000188; suivant : 000190

The 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 :

RBID : PMC:3142614

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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PMC:3142614

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