@article{de:2016:10.1038/nchembio.2147,
author = {de, Saint Germain A and Clavé, G and Badet-Denisot, MA and Pillot, JP and Cornu, D and Le, Caer JP and Burger, M and Pelissier, F and Retailleau, P and Turnbull, C and Bonhomme, S and Chory, J and Rameau, C and Boyer, FD},
doi = {10.1038/nchembio.2147},
journal = {Nature Chemical Biology},
pages = {787--794},
title = {An histidine covalent receptor and butenolide complex mediates strigolactone perception},
url = {http://dx.doi.org/10.1038/nchembio.2147},
volume = {12},
year = {2016}
}

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TY  - JOUR
AB  - 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.
AU  - de,Saint Germain A
AU  - Clavé,G
AU  - Badet-Denisot,MA
AU  - Pillot,JP
AU  - Cornu,D
AU  - Le,Caer JP
AU  - Burger,M
AU  - Pelissier,F
AU  - Retailleau,P
AU  - Turnbull,C
AU  - Bonhomme,S
AU  - Chory,J
AU  - Rameau,C
AU  - Boyer,FD
DO  - 10.1038/nchembio.2147
EP  - 794
PY  - 2016///
SN  - 1552-4469
SP  - 787
TI  - An histidine covalent receptor and butenolide complex mediates strigolactone perception
T2  - Nature Chemical Biology
UR  - http://dx.doi.org/10.1038/nchembio.2147
UR  - http://hdl.handle.net/10044/1/39540
VL  - 12
ER  - 

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