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פותח על ידי קלירמאש פתרונות בע"מ -
Sulfated RaxX, which represents an unclassified group of ribosomally synthesized post-translationally modified peptides, binds a host immune receptor
Year:
2018
Authors :
בהר, אופיר
;
.
Volume :
Co-Authors:

Dee Dee Luu1, , Anna  , Yan Chen , Katarzyna Parys,  Rory Pruitt1, Leanne Jade G. Chen, Christopher J. Petzold , Kelsey Long , Clifford Adamchak , Valley Stewart , Youssef Belkhadir , Pamela C. Ronal,

Facilitators :
From page:
0
To page:
0
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Total pages:
1
)
Abstract:

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.

Note:
Related Files :
peptide
Receptor
עוד תגיות
תוכן קשור
More details
DOI :
https://doi.org/10.1101/442517
Article number:
0
Affiliations:
Database:
גוגל סקולר
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
46188
Last updated date:
02/03/2022 17:27
Creation date:
17/02/2020 13:07
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Scientific Publication
Sulfated RaxX, which represents an unclassified group of ribosomally synthesized post-translationally modified peptides, binds a host immune receptor

Dee Dee Luu1, , Anna  , Yan Chen , Katarzyna Parys,  Rory Pruitt1, Leanne Jade G. Chen, Christopher J. Petzold , Kelsey Long , Clifford Adamchak , Valley Stewart , Youssef Belkhadir , Pamela C. Ronal,

Sulfated RaxX, which represents an unclassified group of ribosomally synthesized post-translationally modified peptides, binds a host immune receptor .

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.

Scientific Publication
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