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Nat Chem Biol. 2016 Oct;12(10):787-794. doi: 10.1038/nchembio.2147. Epub 2016 Aug 1.

An histidine covalent receptor and butenolide complex mediates strigolactone perception.

Author information

1
Institut Jean-Pierre Bourgin, INRA, AgroParisTech, CNRS, Université Paris-Saclay, RD10, 78026 Versailles Cedex, France.
2
Howard Hughes Medical Institute.
3
Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
4
Institut de Chimie des Substances Naturelles, CNRS UPR2301, Univ. Paris-Sud, Université Paris-Saclay, 1 av. de la Terrasse, F-91198 Gif-sur-Yvette, France.
5
Institut de Biologie Intégrative de la Cellule, CNRS, CEA, Univ. Paris-Sud, Université Paris-Saclay, 1 av. de la Terrasse, F-91190 Gif-sur-Yvette, France.
6
Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ, United Kingdom.
#
Contributed equally

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 α/β-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.

PMID:
27479744
PMCID:
PMC5030144
DOI:
10.1038/nchembio.2147
[Indexed for MEDLINE]
Free PMC Article

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