ABSTRACT:The N-terminal region of rice pumilio 1 fused with the binding domain (BD-OsPUM1) was used as a bait construct in yeast two-hybrid screening with a rice cDNA library as prey. Several interacting proteins were screened in a stringent media and tested with beta-galactose filter assay. The nucleotide sequences encoding interacting proteins were determined and annotated according to the rice genome database. These proteins are sigma factor F inhibitor, RPL18C, RUBQ2, RPL24A, RCY1, small nuclear ribonucleoprotein G, transferase hexapeptide repeat-containing protein, dormancyassociated protein, and putative expressed proteins with the accessions NP 001067038 and EEE55952. This study suggested that OsPUM1 protein is associated with several biological processes involved in morphology determination, protein folding and plant immunity.

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-ox1 has high similarities of 92% and 83% with BrFMOgs-ox1 and AtFMOgs-ox1,2,3, respectively, and the gene structure of FMOgs-ox1 is similar to its plant homologues. Quantitative (qPCR) analysis revealed that RsFMOgs-ox1 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-ox1 was also regulated by wounding, notably 1 day after treatment. Subcellular localization in Arabidopsis showed that RsFMOgs-ox1 was localized in the cytoplasm and nuclei. This study allows us to understand something about RsFMOgs-ox1 function in glucosinolate biosynthesis.