Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis

Handle URI:
http://hdl.handle.net/10754/594213
Title:
Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis
Authors:
Zhang, Yanxia; van Dijk, Aalt D J; Scaffidi, Adrian; Flematti, Gavin R.; Hofmann, Manuel; Charnikhova, Tatsiana; Verstappen, Francel; Hepworth, Jo; van der Krol, Sander; Leyser, Ottoline; Smith, Steven M.; Zwanenburg, Binne; Al-Babili, Salim; Ruyter-Spira, Carolien; Bouwmeester, Harro J.
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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Center for Desert Agriculture
Citation:
Zhang Y, van Dijk ADJ, Scaffidi A, Flematti GR, Hofmann M, et al. (2014) Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis. Nat Chem Biol 10: 1028–1033. Available: http://dx.doi.org/10.1038/nchembio.1660.
Publisher:
Springer Nature
Journal:
Nature Chemical Biology
Issue Date:
26-Oct-2014
DOI:
10.1038/nchembio.1660
PubMed ID:
25344813
Type:
Article
ISSN:
1552-4450; 1552-4469
Sponsors:
We thank Y. Wang from the Institute of Genetics and Developmental Biology at the Chinese Academy of Science for the p35s:OsD27:PJTK13 plasmid and K. Yoneyama (Weed Science Center, Utsunomiya University, Utsunomiya, Japan) and T. Asami (Department of Applied Biological Chemistry, The University of Tokyo, Japan) for supplying SL standards. We thank J. Beekwilder and K. Cankar (Plant Research International, Wageningen, the Netherlands) for technical advice on the yeast assays and B. Ramakers (Nijmegen University) for technical support with the CD spectra measurement of CL. We thank A. Reeder from the Centre for Microscopy, Characterisation and Analysis (University of Western Australia (UWA)) and M. Clarke from the Centre for Metabolomics (UWA) for technical assistance and instrument access. We acknowledge funding by the Netherlands Organization for Scientific Research (VICI grant 865.06.002 and equipment grant 834.08.001 to H.J.B.), the Australian Research Council (LP0882775 for A.S. and FT110100304 for G.R.F.) and the UK Biotechnology and Biological Sciences Research Council (for J.H. and O.L.). Research reported in this publication was supported by the King Abdullah University of Science and Technology and was cofinanced by the Centre for BioSystems Genomics, which is part of the Netherlands Genomics Initiative/Netherlands Organization for Scientific Research.
Appears in Collections:
Articles; Center for Desert Agriculture; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorZhang, Yanxiaen
dc.contributor.authorvan Dijk, Aalt D Jen
dc.contributor.authorScaffidi, Adrianen
dc.contributor.authorFlematti, Gavin R.en
dc.contributor.authorHofmann, Manuelen
dc.contributor.authorCharnikhova, Tatsianaen
dc.contributor.authorVerstappen, Francelen
dc.contributor.authorHepworth, Joen
dc.contributor.authorvan der Krol, Sanderen
dc.contributor.authorLeyser, Ottolineen
dc.contributor.authorSmith, Steven M.en
dc.contributor.authorZwanenburg, Binneen
dc.contributor.authorAl-Babili, Salimen
dc.contributor.authorRuyter-Spira, Carolienen
dc.contributor.authorBouwmeester, Harro J.en
dc.date.accessioned2016-01-19T14:43:23Zen
dc.date.available2016-01-19T14:43:23Zen
dc.date.issued2014-10-26en
dc.identifier.citationZhang Y, van Dijk ADJ, Scaffidi A, Flematti GR, Hofmann M, et al. (2014) Rice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesis. Nat Chem Biol 10: 1028–1033. Available: http://dx.doi.org/10.1038/nchembio.1660.en
dc.identifier.issn1552-4450en
dc.identifier.issn1552-4469en
dc.identifier.pmid25344813en
dc.identifier.doi10.1038/nchembio.1660en
dc.identifier.urihttp://hdl.handle.net/10754/594213en
dc.description.abstractStrigolactones (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.en
dc.description.sponsorshipWe thank Y. Wang from the Institute of Genetics and Developmental Biology at the Chinese Academy of Science for the p35s:OsD27:PJTK13 plasmid and K. Yoneyama (Weed Science Center, Utsunomiya University, Utsunomiya, Japan) and T. Asami (Department of Applied Biological Chemistry, The University of Tokyo, Japan) for supplying SL standards. We thank J. Beekwilder and K. Cankar (Plant Research International, Wageningen, the Netherlands) for technical advice on the yeast assays and B. Ramakers (Nijmegen University) for technical support with the CD spectra measurement of CL. We thank A. Reeder from the Centre for Microscopy, Characterisation and Analysis (University of Western Australia (UWA)) and M. Clarke from the Centre for Metabolomics (UWA) for technical assistance and instrument access. We acknowledge funding by the Netherlands Organization for Scientific Research (VICI grant 865.06.002 and equipment grant 834.08.001 to H.J.B.), the Australian Research Council (LP0882775 for A.S. and FT110100304 for G.R.F.) and the UK Biotechnology and Biological Sciences Research Council (for J.H. and O.L.). Research reported in this publication was supported by the King Abdullah University of Science and Technology and was cofinanced by the Centre for BioSystems Genomics, which is part of the Netherlands Genomics Initiative/Netherlands Organization for Scientific Research.en
dc.publisherSpringer Natureen
dc.titleRice cytochrome P450 MAX1 homologs catalyze distinct steps in strigolactone biosynthesisen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentCenter for Desert Agricultureen
dc.identifier.journalNature Chemical Biologyen
dc.contributor.institutionLaboratory of Plant Physiology, Wageningen University, Wageningen, the Netherlandsen
dc.contributor.institutionApplied Bioinformatics, Plant Research International, Wageningen, the Netherlandsen
dc.contributor.institutionSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Australiaen
dc.contributor.institutionFaculty of Biology, University of Freiburg, Freiburg, Germanyen
dc.contributor.institutionDepartment of Biology, University of York, Heslington, York, UKen
dc.contributor.institution1] Department of Biology, University of York, Heslington, York, UK. [2] Sainsbury Laboratory, University of Cambridge, Cambridge, UKen
dc.contributor.institutionRadboud University Nijmegen, Institute for Molecules and Materials, Cluster of Organic Chemistry, Nijmegen, the Netherlandsen
dc.contributor.institution1] Laboratory of Plant Physiology, Wageningen University, Wageningen, the Netherlands. [2] Bioscience, Plant Research International, Wageningen, the Netherlandsen
dc.contributor.institution1] Laboratory of Plant Physiology, Wageningen University, Wageningen, the Netherlands. [2] Centre for Biosystems Genomics, Wageningen, the Netherlandsen
kaust.authorZhang, Yanxiaen

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