SCIRP Mobile Website
Paper Submission

Why Us? >>

  • - Open Access
  • - Peer-reviewed
  • - Rapid publication
  • - Lifetime hosting
  • - Free indexing service
  • - Free promotion service
  • - More citations
  • - Search engine friendly

Free SCIRP Newsletters>>

Add your e-mail address to receive free newsletters from SCIRP.


Contact Us >>

WhatsApp  +86 18163351462(WhatsApp)
Paper Publishing WeChat
Book Publishing WeChat

Article citations


Baumann, K., Venail, J., Berbel, A., et al. (2015) Changing the Spatial Pattern of TFL1 Expression Reveals Its Key Role in the Shoot Meristem in Controlling Arabidopsis Flowering Architecture. Journal of Experimental Botany, 66, 4769.

has been cited by the following article:

  • TITLE: Cloning and Bioinformatics Analysis of Rosa rugosa TFL1 Gene (RrTFL1)

    AUTHORS: Dandan Zhao, Xiao Wei, Leilei Wang, Lanyong Zhao, Xiaoyan Yu

    KEYWORDS: Rosa rugosa, TFL1 Gene, Clone, Biological Analysis

    JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.8 No.6, June 27, 2017

    ABSTRACT: 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.