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Dee Dee Luu, Anna Joe, Rory Pruitt, Kelsey Long, Clifford Adamchak, Pamela C. Ronald  -Department of Plant Pathology, University of California, Davis, bThe Genome Center, University of California, Davis
Yan Chen, Leanne Jade G. Chan, Christopher J. Petzold - Technology Division, Joint Bioenergy Institute, Emeryville, Katarzyna Parys, Youssef Belkhadir - Gregor Mendel Institute, Austrian Academy of Sciences, 1030 Vienna, Austria,
Valley Stewart - Department of Microbiology & Molecular Genetics, University of California, Davis
 

The rice immune receptor XA21 is activated by the sulfated microbial peptide required for activation of XA21-mediated immunity X (RaxX) produced by Xanthomonas oryzae pv. oryzae (Xoo). Mutational studies and targeted proteomics revealed that the RaxX precursor peptide (proRaxX) is processed and secreted by the protease/transporter RaxB, the function of which can be partially fulfilled by a noncognate peptidase-containing transporter component B (PctB). proRaxX is cleaved at a Gly–Gly motif, yielding a mature peptide that retains the necessary elements for RaxX function as an immunogen and host peptide hormone mimic. These results indicate that RaxX is a prokaryotic member of a previously unclassified and understudied group of eukaryotic tyrosine sulfated ribosomally synthesized, posttranslationally modified peptides (RiPPs). We further demonstrate that sulfated RaxX directly binds XA21 with high affinity. This work reveals a complete, previously uncharacterized biological process: bacterial RiPP biosynthesis, secretion, binding to a eukaryotic receptor, and triggering of a robust host immune response.

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Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor
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Dee Dee Luu, Anna Joe, Rory Pruitt, Kelsey Long, Clifford Adamchak, Pamela C. Ronald  -Department of Plant Pathology, University of California, Davis, bThe Genome Center, University of California, Davis
Yan Chen, Leanne Jade G. Chan, Christopher J. Petzold - Technology Division, Joint Bioenergy Institute, Emeryville, Katarzyna Parys, Youssef Belkhadir - Gregor Mendel Institute, Austrian Academy of Sciences, 1030 Vienna, Austria,
Valley Stewart - Department of Microbiology & Molecular Genetics, University of California, Davis
 
Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor .

The rice immune receptor XA21 is activated by the sulfated microbial peptide required for activation of XA21-mediated immunity X (RaxX) produced by Xanthomonas oryzae pv. oryzae (Xoo). Mutational studies and targeted proteomics revealed that the RaxX precursor peptide (proRaxX) is processed and secreted by the protease/transporter RaxB, the function of which can be partially fulfilled by a noncognate peptidase-containing transporter component B (PctB). proRaxX is cleaved at a Gly–Gly motif, yielding a mature peptide that retains the necessary elements for RaxX function as an immunogen and host peptide hormone mimic. These results indicate that RaxX is a prokaryotic member of a previously unclassified and understudied group of eukaryotic tyrosine sulfated ribosomally synthesized, posttranslationally modified peptides (RiPPs). We further demonstrate that sulfated RaxX directly binds XA21 with high affinity. This work reveals a complete, previously uncharacterized biological process: bacterial RiPP biosynthesis, secretion, binding to a eukaryotic receptor, and triggering of a robust host immune response.

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