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dc.contributor.authorDeb, Sohini-
dc.contributor.authorGupta, Mahesh K.-
dc.contributor.authorPatel, Hitendra K.-
dc.contributor.authorSonti, Ramesh V.-
dc.date.accessioned2019-05-21T09:52:55Z-
dc.date.available2019-05-21T09:52:55Z-
dc.date.issued2019-
dc.identifier.citationMolecular Plant Pathology, 20(7): 976-989en_US
dc.identifier.issn1364-3703-
dc.identifier.urihttp://223.31.159.10:8080/jspui/handle/123456789/952-
dc.descriptionAccepted date: 15 May 2019en_US
dc.description.abstractMany bacterial phytopathogens employ effectors secreted through the type-III secretion system to suppress plant innate immune responses. The Xanthomonas type-III secreted non-TAL effector protein Xanthomonas outer protein Q (XopQ) exhibits homology to nucleoside hydrolases. Previous work indicated that mutations which affect the biochemical activity of XopQ fail to affect its ability to suppress rice innate immune responses, suggesting that the effector might be acting through some other pathway or mechanism. In this study, we show that XopQ interacts in yeast and in planta with two rice 14-3-3 proteins, Gf14f and Gf14g. A serine to alanine mutation (S65A) of a 14-3-3 interaction motif in XopQ abolishes the ability of XopQ to interact with the two 14-3-3 proteins and to suppress innate immunity. Surprisingly, the S65A mutant gains the ability to interact with a third 14-3-3 protein that is a negative regulator of innate immunity. The XopQS65A mutant is an inducer of rice immune responses and this property is dominant over the wild-type function of XopQ. Taken together, these results suggest that XopQ targets the rice 14-3-3 mediated immune response pathway and that its differential phosphorylation might enable interaction with alternative 14-3-3 proteins.en_US
dc.description.sponsorshipWe acknowledge Mary B. Mudgett (Stanford University) for providing the BiFC vectors pDEST-VYNE(R)GW and pDESTVYNE(R)GW. This work was supported by grants to RVS from the Plant-Microbe and Soil Interaction (PMSI) project of the Council of Scientific and Industrial Research (CSIR), Government of India and the J. C. Bose fellowship to RVS from the Department of Science and Technology (DST), Government of India. SD acknowledges the Council of Scientific and Industrial Research (CSIR), Government of India for a Ph.D. fellowship. We thank T. Lavanya and S. Pillai for critical reviewing of the manuscript.en_US
dc.language.isoen_USen_US
dc.publisherJohn Wiley & Sonsen_US
dc.subjectXanthomonas oryzae pv. oryzaeen_US
dc.subject14-3-3 proteinen_US
dc.subjectXopQen_US
dc.subjectresistanceen_US
dc.subjectriceen_US
dc.subjecteffectoren_US
dc.titleXanthomonas oryzae pv. oryzae XopQ protein suppresses rice immune responses through interaction with two 14-3-3 proteins but its phospho-null mutant induces rice immune responses and interacts with another 14-3-3 proteinen_US
dc.typeArticleen_US
dc.identifier.officialurlhttps://onlinelibrary.wiley.com/doi/full/10.1111/mpp.12807en_US
dc.identifier.doihttps://doi.org/10.1111/mpp.12807en_US
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