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Identification of a host 14-3-3 Protein that Interacts with Xanthomonas effector AvrRxv.
- Whalen, Maureen;
- Richter, Todd;
- Zakhareyvich, Kseniya;
- Yoshikawa, Masayasu;
- Al-Azzeh, Dana;
- Adefioye, Adeshola;
- Spicer, Greg;
- Mendoza, Laura L;
- Morales, Christine Q;
- Klassen, Vicki;
- Perez-Baron, Gina;
- Toebe, Carole S;
- Tzovolous, Ageliki;
- Gerstman, Emily;
- Evans, Erika;
- Thompson, Cheryl;
- Lopez, Mary;
- Ronald, Pamela C
- et al.
Abstract
AvrRxv is a member of a family of pathogen effectors present in pathogens of both plant and mammalian species. Xanthomonas campestris pv. vesicatoria strains carrying AvrRxv induce a hypersensitive response (HR) in the tomato cultivar Hawaii 7998. Using a yeast two-hybrid screen, we identified a 14-3-3 protein from tomato that interacts with AvrRxv called AvrRxv Interactor 1 (ARI1). The interaction was confirmed in vitro with affinity chromatography. Using mutagenesis, we identified a 14-3-3-binding domain in AvrRxv and demonstrated that a mutant in that domain showed concomitant loss of interaction with ARI1 and HR-inducing activity in tomato. These results demonstrate that the AvrRxv bacterial effector recruits 14-3-3 proteins for its function within host cells. AvrRxv homologues YopP and YopJ from Yersinia do not have AvrRxv-specific HR-inducing activity when delivered into tomato host cells by Agrobacterium. Although YopP itself cannot induce HR, its C-terminal domain containing the catalytic residues can replace that of AvrRxv in an AvrRxv-YopP chimera for HR-inducing activity. Phylogenetic analysis indicates that the sequences encoding the C-termini of family members are evolving independently from those encoding the N-termini. Our results support a model in which there are three functional domains in proteins of the family, translocation, interaction, and catalytic.
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