Journal
NATURE CHEMICAL BIOLOGY
Volume 10, Issue 12, Pages 1028-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nchembio.1660
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Funding
- Netherlands Organization for Scientific Research (VICI) [865.06.002, 834.08.001]
- Australian Research Council [LP0882775, FT110100304]
- UK Biotechnology and Biological Sciences Research Council
- King Abdullah University of Science and Technology
- Centre for BioSystems Genomics
- Netherlands Genomics Initiative/Netherlands Organization for Scientific Research
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Strigolactones (SLs) are a class of phytohormones and rhizosphere signaling compounds with high structural diversity. Three enzymes, carotenoid isomerase DWARF27 and carotenoid cleavage dioxygenases CCD7 and CCD8, were previously shown to convert all-trans-beta-carotene to carlactone (CL), the SL precursor. However, how CL is metabolized to SLs has remained elusive. Here, by reconstituting the SL biosynthetic pathway in Nicotiana benthamiana, we show that a rice homolog of Arabidopsis MORE AXILLARY GROWTH 1 (MAX1), encodes a cytochrome P450 CYP711 subfamily member that acts as a CL oxidase to stereoselectively convert CL into ent-2'-epi-5-deoxystrigol (B-C lactone ring formation), the presumed precursor of rice SLs. A protein encoded by a second rice MAX1 homolog then catalyzes the conversion of ent-2'-epi-5-deoxystrigol to orobanchol. We therefore report that two members of CYP711 enzymes can catalyze two distinct steps in SL biosynthesis, identifying the first enzymes involved in B-C ring closure and a subsequent structural diversification step of SLs.
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