Geranylgeranyl Diphosphate Synthase from Scoparia dulcis and Croton sublyratus. Plastid Localization and Conversion to a Farnesyl Diphosphate Synthase by Mutagenesis.

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  • SITTHITHAWORN Worapan
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • KOJIMA Naoe
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • VIROONCHATAPAN Ekapop
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • SUH Dae-Yeon
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • IWANAMI Naoko
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • HAYASHI Toshimitsu
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University
  • NOJI Masaaki
    Laboratory of Molecular Biology and Biotechnology, Research Center of Medicinal Resources, Faculty of Pharmaceutical Sciences, Chiba University
  • SAITO Kazuki
    Laboratory of Molecular Biology and Biotechnology, Research Center of Medicinal Resources, Faculty of Pharmaceutical Sciences, Chiba University
  • NIWA Yasuo
    Laboratory of Plant Cell Technology, Graduate School of Nutritional and Environmental Sciences, University of Shizuoka
  • SANKAWA Ushio
    Faculty Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University International Traditional Medicine Research Center, Toyama International Health Complex

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cDNAs encoding geranylgeranyl diphosphate synthase (GGPPS) of two diterpene-producing plants, Scoparia dulcis and Croton sublyratus, have been isolated using the homology-based polymerase chain reaction (PCR) method. Both clones contained highly conserved aspartate-rich motifs (DDXX(XX)D) and their N-terminal residues exhibited the characteristics of chloroplast targeting sequence. When expressed in Escherichia coli, both the full-length and truncated proteins in which the putative targeting sequence was deleted catalyzed the condensation of farnesyl diphosphate and isopentenyl diphosphate to produce geranylgeranyl diphosphate (GGPP). The structural factors determining the product length in plant GGPPSs were investigated by constructing S. dulcis GGPPS mutants on the basis of sequence comparison with the first aspartate-rich motif (FARM) of plant farnesyl diphosphate synthase. The result indicated that in plant GGPPSs small amino acids, Met and Ser, at the fourth and fifth positions before FARM and Pro and Cys insertion in FARM play essential roles in determination of product length. Further, when a chimeric gene comprised of the putative transit peptide of the S. dulcis GGPPS gene and a green fluorescent protein was introduced into Arabidopsis leaves by particle gun bombardment, the chimeric protein was localized in chloroplasts, indicating that the cloned S. dulcis GGPPS is a chloroplast protein.

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