Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

Yanxia Zhang, Aalt D J van Dijk, Adrian Scaffidi, Gavin R. Flematti, Manuel Hofmann, Tatsiana Charnikhova, Francel Verstappen, Jo Hepworth, Sander van der Krol, Ottoline Leyser, Steven M. Smith, Binne Zwanenburg, Salim Al-Babili, Carolien Ruyter-Spira, Harro J. Bouwmeester

Research output: Contribution to journalArticlepeer-review

175 Scopus citations

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 (US)
Pages (from-to)1028-1033
Number of pages6
JournalNature Chemical Biology
Volume10
Issue number12
DOIs
StatePublished - Oct 26 2014

Fingerprint Dive into the research topics of 'Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis'. Together they form a unique fingerprint.

Cite this