A microbially derived tyrosine-sulfated peptide mimics a plant peptide hormone

The biotrophic pathogen Xanthomonas oryzae pv. oryzae (Xoo) produces a sulfated peptide named RaxX, which shares similarity to peptides in the PSY (plant peptide containing sulfated tyrosine) family. We hypothesize that RaxX mimics the growth-stimulating activity of PSY peptides. Root length was mea...

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Bibliographic Details
Published in:The New phytologist 2017-07, Vol.215 (2), p.725-736
Main Authors: Pruitt, Rory N., Joe, Anna, Zhang, Weiguo, Feng, Wei, Stewart, Valley, Schwessinger, Benjamin, Dinneny, José R., Ronald, Pamela C.
Format: Article
Language:English
Subjects:
Arabidopsis
Genomic analysis
Growth
Hormones
Immunity
Microorganisms
molecular mimicry
Pathogens
Peptides
Plant bacterial diseases
PSY1
RaxX
Reactive oxygen species
Receptors
Residues
Rice
root growth
Tyrosine
tyrosine‐sulfated peptide
Virulence
XA21
Xanthomonas oryzae pv. oryzae
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Summary:The biotrophic pathogen Xanthomonas oryzae pv. oryzae (Xoo) produces a sulfated peptide named RaxX, which shares similarity to peptides in the PSY (plant peptide containing sulfated tyrosine) family. We hypothesize that RaxX mimics the growth-stimulating activity of PSY peptides. Root length was measured in Arabidopsis and rice treated with synthetic RaxX peptides. We also used comparative genomic analyses and reactive oxygen species burst assays to evaluate the activity of RaxX and PSY peptides. Here we found that a synthetic sulfated RaxX derivative comprising 13 residues (RaxX13-sY), highly conserved between RaxX and PSY, induces root growth in Arabidopsis and rice in a manner similar to that triggered by PSY. We identified residues that are required for activation of immunity mediated by the rice XA21 receptor but that are not essential for root growth induced by PSY. Finally, we showed that a Xanthomonas strain lacking raxX is impaired in virulence. These findings suggest that RaxX serves as a molecular mimic of PSY peptides to facilitate Xoo infection and that XA21 has evolved the ability to recognize and respond specifically to the microbial form of the peptide.
ISSN:0028-646X
1469-8137
DOI:10.1111/nph.14609