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The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.


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.

SUBMITTER: Catanzariti AM 

PROVIDER: S-EPMC3142614 | biostudies-literature | 2010 Jan

REPOSITORIES: biostudies-literature

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The AvrM effector from flax rust has a structured C-terminal domain and interacts directly with the M resistance protein.

Catanzariti Ann-Maree AM   Dodds Peter N PN   Ve Thomas T   Kobe Bostjan B   Ellis Jeffrey G JG   Staskawicz Brian J BJ  

Molecular plant-microbe interactions : MPMI 20100101 1


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 ea  ...[more]

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