Liu, FurongMcDonald, MeganSchwessinger, BenjaminJoe, AnnaPruitt, RoryErickson, TeresaZhao, XiuxiangStewart, ValleyRonald, Pamela2020-01-022020-01-021464-6722http://hdl.handle.net/1885/196470The rice XA21-mediated immune response is activated on recog-nition of the RaxX peptide produced by the bacterium Xanthomonas oryzae pv. oryzae (Xoo). The 60-residue RaxX pre-cursor is post-translationally modified to form a sulfated tyrosine peptide that shares sequence and functional similarity with the plant sulfated tyrosine (PSY) peptide hormones. The 5-kb raxX-raxSTAB gene cluster of Xoo encodes RaxX, the RaxST tyrosyl-protein sulfotransferase, and the RaxA and RaxB components of a predicted type I secretion system. To assess raxX-raxSTAB gene cluster evolution and to determine its phylogenetic distribution, we first identified rax gene homologues in other genomes. We detected the complete raxX-raxSTAB gene cluster only in Xanthomonas spp., in five distinct lineages in addition to X.ory-zae. The phylogenetic distribution of the raxX-raxSTAB gene cluster is consistent with the occurrence of multiple lateral (hori-zontal) gene transfer events during Xanthomonas speciation. RaxX natural variants contain a restricted set of missense substi-tutions, as expected if selection acts to maintain peptide hor-mone-like function. Indeed, eight RaxX variants tested all failed to activate the XA21-mediated immune response, yet retained peptide hormone activity. Together, these observations support the hypothesis that the XA21 receptor evolved specifically to rec-ognize Xoo RaxX.This study was supported by Public Health Service research grants GM059962 and GM122968 from the National Institute of General Medical Sciences awarded to P.C.R.application/pdfen-AU© 2019 The Authors.https://creativecommons.org/licenses/by/4.0/201910.1111/mpp.127832019-08-04Creative Commons Attribution License