Cloning and molecular analysis of radish (Raphanus sativus L.) cDNAs encoding heterodimeric γ-glutamyltransferases

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  • Nakano Yoshihiro
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • Prieto Rafael
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University
  • Hara Masakazu
    Faculty of Agriculture, Shizuoka University
  • Sekiya Jiro
    Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University

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タイトル別名
  • Cloning and molecular analysis of radish (Raphanus sativus L.) cDNAs encoding heterodimeric .GAMMA.-glutamyltransferases
  • Cloning and molecular analysis of radish Raphanus sativus L cDNA s encoding heterodimeric ガンマ glutamyltransferases

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γ-Glutamyltransferase (GGT) catalyzes the hydrolysis and transpeptidation of the γ-glutamyl moiety of γ-glutamyl peptides. Based on the N-terminal amino acid sequences of purified radish heterodimeric GGTs, we cloned and characterized three radish full-length cDNAs (RsGGT1, RsGGT2 and RsGGT3) encoding putative heterodimeric GGT isoforms. RsGGT proteins contained conserved amino acid residues that are required for the catalytic activity and the post-translational processing of GGT proteins in E. coli and mammals. Expression analysis indicated that RsGGT showed different organ expression patterns. The overexpression of RsGGT1 and RsGGT2 cDNAs, but not that of RsGGT3 cDNA, resulted in an increase of NaCl-extractable bound GGT activity in transgenic tobacco plants. These results suggest that RsGGT1 and RsGGT2 cDNAs encode heterodimeric bound GGT isoforms.

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