The AvrM Effector from Flax Rust Has a Structured C-Terminal Domain and Interacts Directly with the M Resistance Protein
| Autor: | Ann-Maree Catanzariti, Peter N. Dodds, Thomas Ve, Bostjan Kobe, Jeffrey G. Ellis, Brian J. Staskawicz |
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| Jazyk: | angličtina |
| Rok vydání: | 2010 |
| Předmět: | |
| Zdroj: | Molecular Plant-Microbe Interactions, Vol 23, Iss 1, Pp 49-57 (2010) |
| Druh dokumentu: | article |
| ISSN: | 1943-7706 0894-0282 |
| DOI: | 10.1094/MPMI-23-1-0049 |
| Popis: | 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. |
| Databáze: | Directory of Open Access Journals |
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