In order to determine if the TFL1 is related with the continuous flowering phenotype of wild Rosa rugosa from Muping, the full-length cDNA sequence of TFL1 Gene was cloned for the first time from the flower buds of wild Rosa rugosafrom Muping with RT-PCR and RACE methods and named as RrTFL1. The full-length cDNA is 973 bp with an open reading frame of 519 bp, encoding 172 amino acids. The derived protein has a molecular weight of 19.48 kD, a calculated pI of 9.13, a c100227 conserved domain at position 1-172, and belongs to PEBP family. The derived protein is a Hydrophilic protein secreted into the cytoplasmic. There is no transmembrane domain and no signal peptide cleavage site, five Ser phosphorylation sites, seven Thr phosphorylation sites, three Tyr phosphorylation sites, one O-glycosylation site, and no N-glycosylation sites. There are 24.42% α-helixes, 36.63% random coil, 27.91% extended peptide chain, and 11.05% β-corner structure. This protein and the TFL1 protein from Rosaceae plants, including Rosa chinensis, share a sequence homology of 87% - 96%. All of the proteins contain a c100227 conserved domain, two highly conserved modules D-P-D-x-P, G-x-H-R, and two functional sites His, Asp. Furthermore, their phylogenetic relationships are consistent with their traditional classifications. These results not only laid a foundation for further researching the expression and function of RrTFL1, but also cultivating new varieties of R. rugosawhich can flower continuously by gene engineering.
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