{"database":"panorama","file_versions":[],"scores":null,"additional":{"omics_type":["Proteomics"],"submitter":["Chris Petzold"],"species":["Xanthomonas Oryzae Pv. Oryzae"],"full_dataset_link":["https://panoramaweb.org/Biosynthesis-and-secretion-RaxX-and-binding-to-rice-XA21.url"],"submitter_email":["cjpetzold@lbl.gov"],"submitter_affiliation":["Lawrence Berkeley National Laboratory"],"sample_protocol":[""],"repository":["PanoramaPublic"],"data_protocol":[""],"pubmed_abstract":["The rice immune receptor XA21 is activated by the sulfated microbial peptide required for activation of XA21-mediated immunity X (RaxX) produced by <i>Xanthomonas oryzae</i> pv. <i>oryzae</i> (<i>Xoo</i>). 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."],"pubmed_title":["Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor."],"pubmed_authors":["Luu Dee Dee DD, Joe Anna A, Chen Yan Y, Parys Katarzyna K, Bahar Ofir O, Pruitt Rory R, Chan Leanne Jade G LJG, Petzold Christopher J CJ, Long Kelsey K, Adamchak Clifford C, Stewart Valley V, Belkhadir Youssef Y, Ronald Pamela C PC"],"pubmed_title_synonyms":["biochemical pathways, single-organism biosynthetic process, bioformation, biodegradation, exocrine gland fluid, peptides, degradation, exocrine gland fluid or secretion, catabolism, anabolism, external secretion, ligand, Oryza sativa, Bodily, Peptide, Rice., exocrine gland fluid/secretion, polypeptide, peptide, Bodily Secretion, secreted substance, Polypeptides, Secretion, red rice <Oryza sativa>, peptido, bodily secretion, Secretions, rice, Rices, red rice, biotransformation, secretion, Peptid, peptidos, Polypeptide, exocrine gland secretion, Asian cultivated rice, multicellular organismal biosynthetic process"],"name_synonyms":["biochemical pathways, single-organism biosynthetic process, bioformation, biodegradation, exocrine gland fluid, peptides, degradation, exocrine gland fluid or secretion, catabolism, anabolism, external secretion, ligand, Oryza sativa, Bodily, Peptide, Rice., exocrine gland fluid/secretion, polypeptide, peptide, Bodily Secretion, secreted substance, Polypeptides, Secretion, red rice <Oryza sativa>, peptido, bodily secretion, Secretions, rice, Rices, red rice, biotransformation, secretion, Peptid, peptidos, Polypeptide, exocrine gland secretion, Asian cultivated rice, multicellular organismal biosynthetic process"],"pubmed_abstract_synonyms":["biochemical pathways, host organism, para Tyrosine, bioformation, single-organism process, exocrine gland fluid, H2N-CH2-COOH, Peptidomics, Proteolytic Enzyme, exocrine gland fluid or secretion, Processes, Aminoessigsaeure, Protease, Gly, precursor, element, Hormone, Esteroproteases, peptide, Polypeptides, Hydrolase, Biological Processes, Biological Phenomenon, peptido, Biological, Rices, Proteases, peptidase, Peptide Hydrolase, Immune., Phenomenon, \"Pseudomonas oryzae\" Uyeda and Ishiyama in Ishiyama 1926, multicellular organismal biosynthetic process, Immune Processes, single-organism biosynthetic process, Immune Responses, G, peptides, catabolism, anabolism, ligand, polypeptide hormone, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Bodily, Y, Proteolytic, Proteinases, set, secreted substance, Enzyme, Secretion, Immune Response, Immune, Glycin, L Tyrosine, bodily secretion, Glycocoll, grupos, Tyr, physiological process, Secretions, biotransformation, peptidos, DAB1, Leimzucker, glycopeptide hormone, Tyrosin, MPRP-1, elements, Immune Process, Asian cultivated rice, atom, Biologic, Proteinase, grupo, ZMPOMA1, Process, peptide hormone, degradation, Hormones, 2010001O09Rik, external secretion, Aminoacetic acid, 2-Amino-3-(p-hydroxyphenyl)propionic acid, single organism process, function, para-Tyrosine, aminoethanoic acid, motif, Peptide, results, group, Tyrosine, polypeptide, exocrine gland fluid/secretion, Bodily Secretion, tirosina, Phenomena, red rice, Peptidases, atomo, atomus, peptide hormones, secretion, Biological Process, atome, biological process, activation, Peptide Hormone, lipopeptide hormone, parent ion, Biologic Phenomena, Element, cAMP generating peptide activity, biodegradation, ensemble, Hgly, atoms, Oryza sativa, L-isomer, Rest, YKR087C, Glyzin, Rice, L isomer, Peptidase, red rice <Oryza sativa>, precursor ion, rice, Glykokoll, Response, Peptid, L-Tyrosine, Polypeptide, Polypeptide Hormone, Polypeptide Hormones, exocrine gland secretion, groupe, Proteolytic Enzymes, Gruppe"],"description_synonyms":["biochemical pathways, host organism, para Tyrosine, bioformation, single-organism process, exocrine gland fluid, H2N-CH2-COOH, Peptidomics, Proteolytic Enzyme, exocrine gland fluid or secretion, Processes, Aminoessigsaeure, Protease, Gly, element, Hormone, Esteroproteases, peptide, Polypeptides, Hydrolase, Biological Processes, Biological Phenomenon, peptido, Biological, Rices, Proteases, peptidase, Peptide Hydrolase, Immune., Phenomenon, multicellular organismal biosynthetic process, Immune Processes, single-organism biosynthetic process, Immune Responses, G, peptides, catabolism, anabolism, ligand, polypeptide hormone, 2-amino-3-(4-hydroxyphenyl)propanoic acid, 3-(p-Hydroxyphenyl)alanine, Bodily, Y, Proteolytic, Proteinases, set, secreted substance, Enzyme, Secretion, Immune Response, Immune, Glycin, L Tyrosine, bodily secretion, Glycocoll, grupos, Tyr, physiological process, Secretions, biotransformation, peptidos, DAB1, Leimzucker, glycopeptide hormone, Tyrosin, MPRP-1, elements, Immune Process, Asian cultivated rice, atom, Biologic, Proteinase, grupo, ZMPOMA1, Process, peptide hormone, degradation, Hormones, 2010001O09Rik, external secretion, Aminoacetic acid, 2-Amino-3-(p-hydroxyphenyl)propionic acid, single organism process, function, para-Tyrosine, aminoethanoic acid, motif, Peptide, results, group, Tyrosine, polypeptide, exocrine gland fluid/secretion, Bodily Secretion, tirosina, Xanthomonas campestris pv. oryza, Phenomena, red rice, Peptidases, atomo, atomus, peptide hormones, secretion, Biological Process, atome, biological process, activation, Peptide Hormone, lipopeptide hormone, Biologic Phenomena, Element, cAMP generating peptide activity, biodegradation, ensemble, Hgly, atoms, Oryza sativa, L-isomer, Rest, YKR087C, Glyzin, Rice, L isomer, Peptidase, red rice <Oryza sativa>, rice, Glykokoll, Response, Peptid, L-Tyrosine, Polypeptide, Polypeptide Hormone, Polypeptide Hormones, exocrine gland secretion, groupe, Proteolytic Enzymes, Gruppe"],"additional_accession":[]},"is_claimable":false,"name":"Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor","description":"The rice immune receptor XA21 is activated by the sulfated microbial peptide RaxX (required for activation of XA21-mediated immunity X) produced by Xanthomonas oryzae pv. oryzae (Xoo). Mutational studies and targeted proteomics revealed that RaxX is processed and secreted by the protease/transporter RaxB, whose function can be partially fulfilled by a noncognate peptidase-containing transporter B (PctB). RaxX 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 founding member of a previously unclassified and understudied group of tyrosine sulfated RiPPs (ribosomally synthesized, post-translationally modified peptides). 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.","dates":{"publication":"Tue Apr 16 00:00:00 GMT+01:00 2019"},"accession":"PXD013389","cross_references":{"TAXONOMY":["64187"],"pubmed":["30948631"]}}