Isolation and expression of FMOgs-oxl from Korean radish

Abstract

Flavin monooxygenase (FMO) is one of the most important enzymes involved in glucosinolate biosynthesis. In this study, the full length of FMO gene (RsFMOgs-ox1) encoding a putative FMO protein composed of 450 amino acids was successfully cloned using the RACE-PCR method. The amino acid sequence of RsFMOgs-oxl has high similarities of 92% and 83% with BrFMOgs-oxl and AtFMOgs-ox1,2,3, respectively, and the gene structure of FMOgs-oxl is similar to its plant homologues. Quantitative (qPCR) analysis revealed that RsFMOgs-oxl was highly expressed during early seedling development. In mature radish, the highest expression was observed in the leaves, while the lowest transcript was evident in the root. The expression of RsFMOgs-oxl was also regulated by wounding, notably 1 day after treatment. Subcellular localization in Arabidopsis showed that RsFMOgs-oxl was localized in the cytoplasm and nuclei. This study allows us to understand something about RsFMOgs-oxl function in glucosinolate biosynthesis.