Natural variation reveals key amino acids in a downy mildew effector that alters recognition specificity by an Arabidopsis resistance gene.

Molecular Plant Pathology
Rebecca L AllenJim L Beynon

Abstract

RPP13, a member of the cytoplasmic class of disease resistance genes, encodes one of the most variable Arabidopsis proteins so far identified. This variability is matched in ATR13, the protein from the oomycete downy mildew pathogen Hyaloperonospora parasitica recognized by RPP13, suggesting that these proteins are involved in tight reciprocal coevolution. ATR13 exhibits five domains: an N-terminal signal peptide, an RXLR motif, a heptad leucine/isoleucine repeat, an 11-amino-acid repeated sequence and a C-terminal domain. We show that the conserved RXLR-containing domain is dispensable for ATR13-mediated recognition, consistent with its role in transport into the plant cytoplasm. Sequencing ATR13 from 16 isolates of H. parasitica revealed high levels of amino acid diversity across the entire protein. The leucines/isoleucines of the heptad leucine repeat were conserved, and mutation of particular leucine or isoleucine residues altered recognition by RPP13. Natural variation has not exploited this route to detection avoidance, suggesting a key role of this domain in pathogenicity. The extensive variation in the 11-amino-acid repeat units did not affect RPP13 recognition. Domain swap analysis showed that recognition specificity l...Continue Reading

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Citations

Dec 5, 2009·Molecular Plant-microbe Interactions : MPMI·Ann-Maree CatanzaritiBrian J Staskawicz
Nov 22, 2011·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Lennart WirthmuellerMark J Banfield
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Aug 9, 2020·Molecular Plant Pathology·Claire Kanja, Kim E Hammond-Kosack
Apr 2, 2021·The Plant Cell·A Cristina Barragan, Detlef Weigel

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