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- W2893223911 abstract "Arbuscular mycorrhizal (AM) fungi form an intimate symbiosis with roots of more than 80% of land plants without eliciting a significant defense response, and how they do so is yet to be determined. Typically, plants mount a defense response upon sensing chitin in fungal walls, and to counteract this response, plant-pathogenic fungi secrete small effector proteins with chitin-binding LysM domains. In the AM fungus, Rhizophagus irregularis, a small, putatively-secreted LysM protein, which we refer to as RiSLM, is among the most highly expressed effector-like proteins during symbiosis. Here, we show that RiSLM expression is reduced during non-functional symbiosis with Medicago mutants, mtpt4-2 and vapyrin. We demonstrate that RiSLM can bind to both chitin and chitosan, and we model the protein-ligand interaction to identify possible binding sites. Finally, we have identified RiSLM homologs in five published R. irregularis isolate genomes and demonstrate that the gene is subject to a high rate of evolution and is experiencing positive selection, while still conserving putative function. Our results present important clues for elucidating a role for a LysM effector, RiSLM, in AM symbiosis." @default.
- W2893223911 created "2018-10-05" @default.
- W2893223911 creator A5005319312 @default.
- W2893223911 creator A5028371168 @default.
- W2893223911 creator A5080481137 @default.
- W2893223911 date "2019-01-01" @default.
- W2893223911 modified "2023-10-14" @default.
- W2893223911 title "A short LysM protein with high molecular diversity from an arbuscular mycorrhizal fungus, Rhizophagus irregularis" @default.
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- W2893223911 doi "https://doi.org/10.1016/j.myc.2018.09.002" @default.
- W2893223911 hasPublicationYear "2019" @default.
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