Claim · model-written summary
Polymorphic AvrP variant residues map to the protein surface and may relate to recognition specificity.
- Taxon
- Melampsora lini
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Melampsora linit0 - Gene
- AvrPe0
- Outcome
- map to the protein surfacee0
- Qualifier
- could be associated with differences in recognition specificitye0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
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Verbatim
e0“Polymorphic residues in AvrP and its allelic variants map to the protein surface and could be associated with differences in recognition specificity.”
t0“Melampsora lini effector AvrP”
t1“Melampsora lini effector AvrP”
Title
Xiaoxiao Zhang; Nadya Farah; Laura Rolston; et al. Molecular Plant Pathology 2017. doi:10.1111/mpp.12597
Other claims from this paper (6)
- Observation AvrP has an elongated zinc finger like structure with a novel interleaved zinc binding topology.
- Observation Zinc binding residues are conserved across AvrP variants.
- Intervention effect Mutation of zinc binding motifs abolished P mediated recognition.
- Observation The first zinc coordinating region has a positively charged surface and limited similarity to nucleic acid binding and chromatin associated proteins.
- Observation Most transiently expressed AvrP accumulated in the Nicotiana benthamiana nucleus.
- Intervention effect Several mutations on the nonconserved AvrP surface patch caused loss of P recognition.