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Rice cytochrome P450 ​MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

Bibliography:

Zhang, Y., van Dijk, A.D.J., Scaffidi, A.,  Flematti, G. R.,  Hofmann, M., Charnikhova, T., Verstappen, F., Hepworth, J., van der Krol, S., Leyser, O., Smith, S.M., Zwanenburg, B., Al-Babili, S., Ruyter-Spira, C. and Bouwmeester, H.J, Rice cytochrome P450 ​MAX1 homologs catalyze distinct steps in strigolactone biosynthesis (2014). Nature Chemical Biology 10, 1028–1033 (2014) doi:10.1038/nchembio.1660

Authors:

Zhang, Y., van Dijk, A.D.J., Scaffidi, A., Flematti, G. R., Hofmann, M., Charnikhova, T., Verstappen, F., Hepworth, J., van der Krol, S., Leyser, O., Smith, S.M., Zwanenburg, B., Al-Babili, S., Ruyter-Spira, C. and Bouwmeester, H.J

Keywords:

Biosynthesis, Enzymes, Natural products, Plant hormones

Year:

2014

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-carotenetocarlactone (​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 ofent-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.

ISSN:

1552-4469