TY - JOUR
T1 - Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis
AU - Zhang, Y.
AU - Van Dijk, A.D.J.
AU - Scaffidi, Adrian
AU - Flematti, Gavin
AU - Hofmann, M.
AU - Charnikhova, T.
AU - Verstappen, F.
AU - Hepworth, J.
AU - Van Der Krol, S.
AU - Leyser, O.
AU - Smith, Steve
AU - Zwanenburg, B.
AU - Al-Babili, S.
AU - Ruyter-Spira, C.
AU - Bouwmeester, H.J.
PY - 2014/12
Y1 - 2014/12
N2 - 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.
AB - 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.
UR - https://www.scopus.com/pages/publications/84921022340
U2 - 10.1038/nchembio.1660
DO - 10.1038/nchembio.1660
M3 - Article
C2 - 25344813
SN - 1552-4450
VL - 10
SP - 1028
EP - 1033
JO - Nature Chemical Biology
JF - Nature Chemical Biology
IS - 12
ER -