Gene_locus Report for: pea-RMS3

Involved in strigolactone signaling pathway. Functions downstream of strigolactone synthesis, as a component of hormone signaling and as an enzyme that participates in the conversion of strigolactones to the bioactive form. Binds and hydrolyzes the synthetic strigolactone analog GR24 and its enantiomers in vitro. Forms a stable covalent complex with the D-ring of strigolactone, which is essential for hormone bioactivity. The D-ring is attached to His-247 of the catalytic triad. The hydrolysis of strigolactone into a covalently linked intermediate molecule is required to trigger strigolactone signaling. This mechanism defines RMS3 as a non-canonical hormone receptor with dual functions to generate and sense the active form of strigolactone

(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.)
> cellular organisms: N E > Eukaryota: N E > Viridiplantae: N E > Streptophyta: N E > Streptophytina: N E > Embryophyta: N E > Tracheophyta: N E > Euphyllophyta: N E > Spermatophyta: N E > Magnoliophyta: N E > Mesangiospermae: N E > eudicotyledons: N E > Gunneridae: N E > Pentapetalae: N E > rosids: N E > fabids: N E > Fabales: N E > Fabaceae: N E > Papilionoideae: N E > Fabeae: N E > Pisum: N E > Pisum sativum: N E

Carboxypeptidase_S10 : pissa-cpaPisum sativum putative serine carboxypeptidase CP-A protein (cp-a gene).
Plant_carboxylesterase : pissa-Q9SSY8Pisum sativum (Garden pea) PsE86 hsr203j homolog.
RsbQ-like : pea-KAI2APisum sativum (Garden pea) Strigolactone esterase, KAI2A Psat2g169960 PsKAI2A, pea-KAI2B Pisum sativum (Garden pea) Strigolactone esterase, KAI2B Psat4g083040 PsKAI2B, pea-KAI2CPisum sativum (Garden pea) Strigolactone esterase, KAI2C Psat3g014200 PsKAI2C.
TGL-GrainShapeFactor : pea-a0a9d4zt76Pisum sativum (Garden pea). AB hydrolase-1 domain-containing protein

Title: An histidine covalent receptor and butenolide complex mediates strigolactone perception
de Saint Germain A, Clave G, Badet-Denisot MA, Pillot JP, Cornu D, Le Caer JP, Burger M, Pelissier F, Retailleau P and Boyer FD <4 more author(s)> de Saint Germain A, Clave G, Badet-Denisot MA, Pillot JP, Cornu D, Le Caer JP, Burger M, Pelissier F, Retailleau P, Turnbull C, Bonhomme S, Chory J, Rameau C, Boyer FD (- 4)
Ref: Nat Chemical Biology, 12:787, 2016 : PubMed
Abstract


ESTHER: de Saint Germain_2016_Nat.Chem.Biol_12_787
PubMedSearch: de Saint Germain 2016 Nat.Chem.Biol 12 787
PubMedID: 27479744
Gene_locus related to this paper: pea-RMS3

Abstract

Strigolactone plant hormones control plant architecture and are key players in both symbiotic and parasitic interactions. They contain an ABC tricyclic lactone connected to a butenolide group, the D ring. The DWARF14 (D14) strigolactone receptor belongs to the superfamily of alpha/beta-hydrolases, and is known to hydrolyze the bond between the ABC lactone and the D ring. Here we characterized the binding and catalytic functions of RAMOSUS3 (RMS3), the pea (Pisum sativum) ortholog of rice (Oryza sativa) D14 strigolactone receptor. Using new profluorescent probes with strigolactone-like bioactivity, we found that RMS3 acts as a single-turnover enzyme that explains its apparent low enzymatic rate. We demonstrated the formation of a covalent RMS3-D-ring complex, essential for bioactivity, in which the D ring was attached to histidine 247 of the catalytic triad. These results reveal an undescribed mechanism of plant hormone reception in which the receptor performs an irreversible enzymatic reaction to generate its own ligand.