摘要
Glycosylation modification fulfills an important role in increasing the stability and solubility of anthocyanin in plants. In this study, based on the transcriptional database of R. rugosa, a gene with full length cDNA of 1161 bp, encoding 386 amino acids, designated as RrGT1, was isolated from flowers of R. rugosa ‘Zizhi’ and then functionally characterized. According to online software prediction, the molecular formula of the protein encoded by the RrGT1 gene is C1879H2964N494O556S14, the relative molecular mass is 41,820.02 Da, and the theoretical isoelectric point is pI = 5.03. The result of the RrGT1 protein 3D model construction showed that it had the highest homology with the UDP-glucose: anthocyanidin 3-O-glucosyltransferase protein model in the database (47.01%). Sequence alignments with the NCBI database showed that the RrGT1 protein is a member of the GTB superfamily. Homology analysis revealed that the coding regions of RrGT1 was highly specific among different species, but still had typical conserved amino acid residues called PSPG that are crucial for RrGT1 enzyme activity. RrGT1 transcripts were detected in five flowering stages and seven tissues of R. rugosa ‘Zizhi’, R. rugosa ‘Fenzizhi’ and R. rugosa ‘Baizizhi’, and their expression patterns corresponded with the accumulation of anthocyanins. Therefore, we speculated that glycosylation of RrGT1 plays a crucial role in anthocyanin biosynthesis in R. rugosa.
Glycosylation modification fulfills an important role in increasing the stability and solubility of anthocyanin in plants. In this study, based on the transcriptional database of R. rugosa, a gene with full length cDNA of 1161 bp, encoding 386 amino acids, designated as RrGT1, was isolated from flowers of R. rugosa ‘Zizhi’ and then functionally characterized. According to online software prediction, the molecular formula of the protein encoded by the RrGT1 gene is C1879H2964N494O556S14, the relative molecular mass is 41,820.02 Da, and the theoretical isoelectric point is pI = 5.03. The result of the RrGT1 protein 3D model construction showed that it had the highest homology with the UDP-glucose: anthocyanidin 3-O-glucosyltransferase protein model in the database (47.01%). Sequence alignments with the NCBI database showed that the RrGT1 protein is a member of the GTB superfamily. Homology analysis revealed that the coding regions of RrGT1 was highly specific among different species, but still had typical conserved amino acid residues called PSPG that are crucial for RrGT1 enzyme activity. RrGT1 transcripts were detected in five flowering stages and seven tissues of R. rugosa ‘Zizhi’, R. rugosa ‘Fenzizhi’ and R. rugosa ‘Baizizhi’, and their expression patterns corresponded with the accumulation of anthocyanins. Therefore, we speculated that glycosylation of RrGT1 plays a crucial role in anthocyanin biosynthesis in R. rugosa.
