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  • Title: Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor.
    Author: Luu DD, Joe A, Chen Y, Parys K, Bahar O, Pruitt R, Chan LJG, Petzold CJ, Long K, Adamchak C, Stewart V, Belkhadir Y, Ronald PC.
    Journal: Proc Natl Acad Sci U S A; 2019 Apr 23; 116(17):8525-8534. PubMed ID: 30948631.
    Abstract:
    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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