HOMEPRODUCTSCOMPANYCONTACTFAQResearchDictionaryPharmaSign Up FREE or Login

The tyrosine-sulfated peptide receptors PSKR1 and PSY1R modify the immunity of Arabidopsis to biotrophic and necrotrophic pathogens in an antagonistic manner.

Abstract
The tyrosine-sulfated peptides PSKα and PSY1 bind to specific leucine-rich repeat surface receptor kinases and control cell proliferation in plants. In a reverse genetic screen, we identified the phytosulfokine (PSK) receptor PSKR1 as an important component of plant defense. Multiple independent loss-of-function mutants in PSKR1 are more resistant to biotrophic bacteria, show enhanced pathogen-associated molecular pattern responses and less lesion formation after infection with the bacterial pathogen Pseudomonas syringae pv. tomato DC3000. By contrast, pskr1 mutants are more susceptible to necrotrophic fungal infection with Alternaria brassicicola, show more lesion formation and fungal growth which is not observed on wild-type plants. The antagonistic effect on biotrophic and necrotrophic pathogen resistance is reflected by enhanced salicylate and reduced jasmonate responses in the mutants, suggesting that PSKR1 suppresses salicylate-dependent defense responses. Detailed analysis of single and multiple mutations in the three paralogous genes PSKR1, -2 and PSY1-receptor (PSY1R) determined that PSKR1 and PSY1R, but not PSKR2, have a partially redundant effect on plant immunity. In animals and plants, peptide sulfation is catalyzed by a tyrosylprotein sulfotransferase (TPST). Mutants lacking TPST show increased resistance to bacterial infection and increased susceptibility to fungal infection, mimicking the triple receptor mutant phenotypes. Feeding experiments with PSKα in tpst-1 mutants partially restore the defense-related phenotypes, indicating that perception of the PSKα peptide has a direct effect on plant defense. These results suggest that the PSKR subfamily integrates growth-promoting and defense signals mediated by sulfated peptides and modulates cellular plasticity to allow flexible adjustment to environmental changes.
AuthorsStephen Mosher, Heike Seybold, Patricia Rodriguez, Mark Stahl, Kelli A Davies, Sajeewani Dayaratne, Santiago A Morillo, Michael Wierzba, Bruno Favery, Harald Keller, Frans E Tax, Birgit Kemmerling
JournalThe Plant journal : for cell and molecular biology (Plant J) Vol. 73 Issue 3 Pg. 469-82 (Feb 2013) ISSN: 1365-313X [Electronic] England
PMID23062058 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Copyright© 2012 The Authors The Plant Journal © 2012 Blackwell Publishing Ltd.
Chemical References
  • Receptors, Peptide
  • Sulfates
  • Tyrosine
Topics
  • Arabidopsis (immunology, microbiology)
  • Receptors, Peptide (chemistry, physiology)
  • Sulfates (chemistry)
  • Tyrosine (chemistry)

Join CureHunter, for free Research Interface BASIC access!

Take advantage of free CureHunter research engine access to explore the best drug and treatment options for any disease. Find out why thousands of doctors, pharma researchers and patient activists around the world use CureHunter every day.
Realize the full power of the drug-disease research graph!


Choose Username:
Email:
Password:
Verify Password:
Enter Code Shown: