Cloning and Analysis of <i>RrF</i>3’ <i>H</i> in <i>Rosa rugosa</i>
- 1 College of Forestry, Shandong Agricultural University, Taian, China
- 2 College of Forestry, Shandong Agricultural University, Taian, China
- 3 College of Forestry, Shandong Agricultural University, Taian, China
- 4 College of Forestry, Shandong Agricultural University, Taian, China
Abstract
Rosa rugosa is an important garden ornamental plant which belongs to the genus Rosa of the family Rosaceae . The current wild and cultivated R. rugosa are mostly purple, pink, a small amount of white, but lack of yellow, orange and so on. Flavonoids 3’-hydroxylase belongs to CYP75B subfamily of cytochrome P450, and is an essential enzyme in anthocyanins synthesis. In this experiment, RrF 3’ H gene was cloned from the petal of Rosa rugosa ‘Hunchun’ using RT-PCR, and bioinformatics analysis was performed. The RrF 3’ H gene’s full length of opening reading frame was 1687 bp, encoding 510 amino acids. The formulas of proteins encoded by RrF 3’ H were C 2666 H 4149 N 699 O 734 S 24 . The derived protein had a molecular weight of 58,506.95 Da. The aliphatic index was 90.94. It belongs to unstable hydrophilic protein. The protein consists of 46.76% α-helix, 31.04% random coil, 7.66% β -corner and 14.54% extended strand. The protein contains 21 Ser phosphorylation sites, 12 Thr phosphorylation sites, and 2 Tyr phosphorylation sites. The protein contained two O-glycosylation sites, located at positions 98 and 263 of the amino acid sequence respectively. The protein has a signal peptide site and a transmembrane structure. In addition, by comparing the expression levels of RrF 3’ H , we found RrF 3’ H was positively correlated with the depth of flower color.
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