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Title: 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.
Authors:
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Publication Date:
Grant/Contract Number:
AC02-05CH11231
Type:
Published Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Name: Proceedings of the National Academy of Sciences of the United States of America; Journal ID: ISSN 0027-8424
Publisher:
Proceedings of the National Academy of Sciences
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
OSTI Identifier:
1505236

Luu, Dee Dee, Joe, Anna, Chen, Yan, Parys, Katarzyna, Bahar, Ofir, Pruitt, Rory, Chan, Leanne Jade G., Petzold, Christopher J., Long, Kelsey, Adamchak, Clifford, Stewart, Valley, Belkhadir, Youssef, and Ronald, Pamela C.. Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor. United States: N. p., Web. doi:10.1073/pnas.1818275116.
Luu, Dee Dee, Joe, Anna, Chen, Yan, Parys, Katarzyna, Bahar, Ofir, Pruitt, Rory, Chan, Leanne Jade G., Petzold, Christopher J., Long, Kelsey, Adamchak, Clifford, Stewart, Valley, Belkhadir, Youssef, & Ronald, Pamela C.. Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor. United States. doi:10.1073/pnas.1818275116.
Luu, Dee Dee, Joe, Anna, Chen, Yan, Parys, Katarzyna, Bahar, Ofir, Pruitt, Rory, Chan, Leanne Jade G., Petzold, Christopher J., Long, Kelsey, Adamchak, Clifford, Stewart, Valley, Belkhadir, Youssef, and Ronald, Pamela C.. 2019. "Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor". United States. doi:10.1073/pnas.1818275116.
@article{osti_1505236,
title = {Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor},
author = {Luu, Dee Dee and Joe, Anna and Chen, Yan and Parys, Katarzyna and Bahar, Ofir and Pruitt, Rory and Chan, Leanne Jade G. and Petzold, Christopher J. and Long, Kelsey and Adamchak, Clifford and Stewart, Valley and Belkhadir, Youssef and Ronald, Pamela C.},
abstractNote = {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.},
doi = {10.1073/pnas.1818275116},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = ,
volume = ,
place = {United States},
year = {2019},
month = {4}
}

Works referenced in this record:

Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension
journal, April 1989

WebLogo: A Sequence Logo Generator
journal, May 2004
  • Crooks, Gavin E.; Hon, Gary; Chandonia, John-Marc
  • Genome Research, Vol. 14, Issue 6, p. 1188-1190
  • DOI: 10.1101/gr.849004