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dc.contributor.authorCarter, Morgan E
dc.contributor.authorHelm, Matthew
dc.contributor.authorChapman, Antony
dc.contributor.authorWan, Emily
dc.contributor.authorRestrepo Sierra, Ana M.
dc.contributor.authorInnes, Roger
dc.contributor.authorBogdanove, Adam J
dc.contributor.authorWise, Roger Philip
dc.date.accessioned2018-12-31T14:01:57Z
dc.date.available2018-12-31T14:01:57Z
dc.date.issued2018-11-27
dc.identifier.citationCarter ME, Helm M, Chapman A, Wan E, Restrepo Sierra AM, et al. (2018) Convergent evolution of effector protease recognition by Arabidopsis and barley. Molecular Plant-Microbe Interactions. Available: http://dx.doi.org/10.1094/mpmi-07-18-0202-fi.
dc.identifier.issn0894-0282
dc.identifier.doi10.1094/mpmi-07-18-0202-fi
dc.identifier.urihttp://hdl.handle.net/10754/630650
dc.description.abstractThe Pseudomonas syringae cysteine protease AvrPphB activates the Arabidopsis resistance protein RPS5 by cleaving a second host protein, PBS1. AvrPphB induces defense responses in other plant species, but the genes and mechanisms mediating AvrPphB recognition in those species have not been defined. Here, we show that AvrPphB induces defense responses in diverse barley cultivars. We show also that barley contains two PBS1 orthologs, that their products are cleaved by AvrPphB, and that the barley AvrPphB response maps to a single locus containing a nucleotide-binding leucine-rich repeat (NLR) gene, which we termed AvrPphB Resistance 1 (Pbr1). Transient co-expression of PBR1 with wild-type AvrPphB, but not a protease inactive mutant, triggered defense responses, indicating that PBR1 detects AvrPphB protease activity. Additionally, PBR1 co-immunoprecipitated with barley and N. benthamiana PBS1 proteins, suggesting mechanistic similarity to detection by RPS5. Lastly, we determined that wheat cultivars also recognize AvrPphB protease activity and contain two putative Pbr1 orthologs. Phylogenetic analyses showed however that Pbr1 is not orthologous to RPS5. Our results indicate that the ability to recognize AvrPphB evolved convergently, and imply that selection to guard PBS1-like proteins occurs across species. Also, these results suggest that PBS1-based decoys may be used to engineer protease effector recognition-based resistance in barley and wheat. .
dc.publisherScientific Societies
dc.relation.urlhttps://apsjournals.apsnet.org/doi/10.1094/MPMI-07-18-0202-FI
dc.titleConvergent evolution of effector protease recognition by Arabidopsis and barley
dc.typeArticle
dc.contributor.departmentStructural Biology and Engineering
dc.identifier.journalMolecular Plant-Microbe Interactions
dc.contributor.institutionCornell University, Plant Pathology and Plant-Microbe Biology Section, School of Integrative Plant Science, 334 Plant Science, 236 Tower Rd, Ithaca, New York, United States, 14850;
dc.contributor.institutionDepartment of Biology, 915 East 3rd Street, Myers Hall 150, Mailbox 62, Bloomington, Indiana, United States, 47405, ;
dc.contributor.institutionIowa State University, Plant Pathology and Microbiology, Ames, Iowa, United States;
dc.contributor.institutionCornell University, Plant Pathology and Plant-Microbe Biology Section, School of Integrative Plant Science, Ithaca, New York, United States;
dc.contributor.institutionIndiana University, Department of Biology, 915 East Third Street, Myers Hall 150, Bloomington, Indiana, United States, 47405-7107, , ;
dc.contributor.institutionCornell University, Plant Pathology and Plant-Microbe Biology Section, School of Integrative Plant Science, 334 Plant Science, Ithaca, New York, United States, 14853;
dc.contributor.institutionIowa State University, Plant Pathology, 351 Besey Hall, Ames, Iowa, United States, 50011-1020, , ;
kaust.personRestrepo Sierra, Ana M.


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