Journal
NATURE CHEMICAL BIOLOGY
Volume 12, Issue 10, Pages 787-+Publisher
NATURE RESEARCH
DOI: 10.1038/nchembio.2147
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Funding
- Institut National de la Recherche Agronomique (INRA)
- Agence Nationale de la Recherche [ANR-12-BSV6-004-01]
- Stream COST Action [FA1206]
- US National Institutes of Health [R01 GM094428]
- Howard Hughes Medical Institute
- Catharina Foundation
- Labex Saclay Plant Sciences-SPS [ANR-10-LABX-0040-SPS]
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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.
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