Molecular cloning and Tissue Distribution of Farnesyl Pyrophosphate Synthase from the Silkworm Bombyx mori

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  • Kikuchi Kyoko
    Development and Differentiation Department, National Institute of Agrobiological Sciences
  • Hirai Makoto
    Development and Differentiation Department, National Institute of Agrobiological Sciences Present address: Jichi Medical School
  • Shiotsuki Takahiro
    Development and Differentiation Department, National Institute of Agrobiological Sciences

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  • Molecular Cloning and Tissue Distribution of Farnesyl Pyrophosphate Synthase from the Silkworm <i>Bombyx mori</i>

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cDNA of farnesyl pyrophosphate synthase (FPS; EC 2.5.1.10), a key enzyme in the formation of the sesquiterpene skeleton of the juvenile hormone (JH) was cloned from the silkworm Bombyx mori (BmFPS). BmFPS cDNA consists of 1743 nucleotides that encode 427 amino acids. Sequence analysis showed that BmFPS has two well-conserved FPS motifs of the five conserved in other FPSs; BmFPS shares 83% identity with the black cutworm moth Agrotis ipsilon, 49% with the fruit fly, Drosophila melanogaster, and 42% with the chicken, Gallus gallus. Analysis of BmFPS gene expression using RT-PCR revealed BmFPS to be distributed throughout tissues with some differences in magnitude. This contradicts our expectation that BmFPS is localized in the corpora allata. BmFPS could therefore catalyze isoprenylation of protein occurring in many tissues.

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