Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

Y. Zhang, A.D.J. Van Dijk, Adrian Scaffidi, Gavin Flematti, M. Hofmann, T. Charnikhova, F. Verstappen, J. Hepworth, S. Van Der Krol, O. Leyser, Steve Smith, B. Zwanenburg, S. Al-Babili, C. Ruyter-Spira, H.J. Bouwmeester

Research output: Contribution to journalArticle

184 Citations (Scopus)

Abstract

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-β-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.
Original languageEnglish
Pages (from-to)1028-1033
JournalNature Chemical Biology
Volume10
Issue number12
Early online date26 Oct 2014
DOIs
Publication statusPublished - Dec 2014

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