Phosphorylation of the alpha-I motif in SYMRK drives root nodule organogenesis.
SYMRK
phosphorylation
plant signaling
plant–microbe interaction
root nodule symbiosis
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
20 Feb 2024
20 Feb 2024
Historique:
medline:
16
2
2024
pubmed:
16
2
2024
entrez:
16
2
2024
Statut:
ppublish
Résumé
Symbiosis receptor-like kinase SYMRK is required for root nodule symbiosis between legume plants and nitrogen-fixing bacteria. To understand symbiotic signaling from SYMRK, we determined the crystal structure to 1.95 Å and mapped the phosphorylation sites onto the intracellular domain. We identified four serine residues in a conserved "alpha-I" motif, located on the border between the kinase core domain and the flexible C-terminal tail, that, when phosphorylated, drives organogenesis. Substituting the four serines with alanines abolished symbiotic signaling, while substituting them with phosphorylation-mimicking aspartates induced the formation of spontaneous nodules in the absence of bacteria. These findings show that the signaling pathway controlling root nodule organogenesis is mediated by SYMRK phosphorylation, which may help when engineering this trait into non-legume plants.
Identifiants
pubmed: 38363863
doi: 10.1073/pnas.2311522121
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2311522121Subventions
Organisme : Novo Nordisk Fonden (NNF)
ID : NNF19SA0059362
Organisme : Bill and Melinda Gates Foundation (GF)
ID : OPP11772165
Organisme : Villum Fonden (Villum Foundation)
ID : 7292
Organisme : Novo Nordisk Fonden (NNF)
ID : NNF20OC0061575
Déclaration de conflit d'intérêts
Competing interests statement:Some findings in this manuscript are considered for patent application.