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פותח על ידי קלירמאש פתרונות בע"מ -
Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor
Year:
2019
Authors :
בהר, אופיר
;
.
Volume :
16
Co-Authors:
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
 
Facilitators :
From page:
8525
To page:
8534
(
Total pages:
10
)
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.

Note:
Related Files :
biosynthesis
peptide
Receptor
rice
Xa21
עוד תגיות
תוכן קשור
More details
DOI :
Article number:
0
Affiliations:
Database:
גוגל סקולר
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
46181
Last updated date:
02/03/2022 17:27
Creation date:
17/02/2020 12:11
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Scientific Publication
Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor
16
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.

Scientific Publication
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