Characterization of a dynamic metabolon producing the defense compound dhurrin in sorghum

Author:

Laursen Tomas12345,Borch Jonas26,Knudsen Camilla1234,Bavishi Krutika1234,Torta Federico7,Martens Helle Juel4,Silvestro Daniele4,Hatzakis Nikos S.28,Wenk Markus R.79,Dafforn Timothy R.1011,Olsen Carl Erik123,Motawia Mohammed Saddik1234,Hamberger Björn12,Møller Birger Lindberg123412,Bassard Jean-Etienne1234

Affiliation:

1. Plant Biochemistry Laboratory, Department of Plant and Environmental Science, University of Copenhagen, DK-1871 Frederiksberg C, Denmark.

2. bioSYNergy, Center for Synthetic Biology, DK-1871 Frederiksberg C, Denmark.

3. VILLUM Research Center for Plant Plasticity, DK-1871 Frederiksberg C, Denmark.

4. Copenhagen Plant Science Center, University of Copenhagen, DK-1871 Frederiksberg C, Denmark.

5. Feedstocks Division, Joint BioEnergy Institute, Emeryville, CA 94608, USA.

6. VILLUM Center For Bioanalytical Sciences, Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense M, Denmark.

7. Department of Biochemistry, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore.

8. Department of Chemistry, Nano-Science Center, University of Copenhagen, DK-2100 Copenhagen, Denmark.

9. Department of Biological Sciences, Yong Loo Lin School of Medicine, National University of Singapore, Singapore 117597, Singapore.

10. School of Biosciences, University of Birmingham, Birmingham B15 2TT, UK.

11. Department of Business, Energy and Industrial Strategy, Her Majesty’s Government, UK.

12. Carlsberg Research Laboratory, DK-1799 Copenhagen V, Denmark.

Abstract

Metabolite channeling by a dynamic metabolon The specialized metabolite dhurrin breaks down into cyanide when plant cell walls have been chewed, deterring insect pests. Laursen et al. found that the enzymes that synthesize dhurrin in sorghum assemble as a metabolon in lipid membranes (see the Perspective by Dsatmaichi and Facchini). The dynamic nature of metabolon assembly and disassembly provides dhurrin on an as-needed basis. Membrane-anchored cytochrome P450s cooperated with a soluble glucosyltransferase to channel intermediates toward efficient dhurrin production. Science , this issue p. 890 ; see also p. 829

Funder

VILLUM Research Center for Plant Plasticity

Center for Synthetic Biology

European Research Council

VILLUM Foundation Young Investigator Programme

European Union's 7th Framework Programme

Innovation Fund Denmark

National Research Foundation of Singapore

Biomedical Research Council-Science and Engineering Research Council

Biological and Biotechnology Science Research Council

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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