Plant Diversity ›› 2015, Vol. 37 ›› Issue (01): 71-77.DOI: 10.7677/ynzwyj201514057

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Cloning and Bioinformatics Analysis of VdAS1 Gene in Vaccinium dunalianum (Ericaceae)

 DU  Wei-1, DING  Yong-1**, ZHU  Dong-Yang-2, YIN  Ji-Ting-2, LIU  Xiao-Zhu-1, ZHAO  Ping-2   

  1. 1 College of Life Sciences, Southwest Forestry University, Kunming 650224, China; 2 Key Laboratory for Forest
    Resources Conservation and Use in the Southwest Mountains of China, Ministry of Education,
    Southwest Forestry University, Kunming 650224, China
  • Received:2014-04-03 Online:2015-01-25 Published:2014-06-13
  • Supported by:

    国家自然科学基金地区科学基金项目 (21462040, 31460076);云南省优势特色重点学科生物学一级学科建设项目 (50097505)


Arbutin was widely used in cosmetics as a whitening agent because of blocking the synthesis of melanin as the inhibitor of tyrosinase. Arbutin synthase (AS) as one member of UDP glycosyltransferases (UGTs) which belongs to the glycosyltransferase (GTs) family is a ratelimiting enzyme in arbutin synthesis from hydroquinone. To reveal the biological function and provide scientific basis of application on plant genetic engineering for Vaccinium dunalianum arbutin synthase (VdAS), a gene VdAS1 encoding VdAS1 was isolated by RTPCR combined with RACEPCR from Vdunalianum. The fulllength cDNA clone comprised 1577 nucleotides consisting of a 17nucleotide 5′untranslated region, an open reading frame of 1428 nucleotides, and a 132nucleotide 3′untranslated region. The open reading frame encoded a putative VdAS1 comprising 475 amino acid residues with molecular weight of 5222kD. and isoelectric point of 574. The total numbers of negative charged residues (Asp+Glu) and positive charged residues (Arg+Lys) in VdAS1 were 53 and 45, respectively. VdAS1 shares 74% similarity with UGT in wolfberry (Lycium barbarum). It was predictive VdAS1 had no signal peptide and transmembrane structure. The main parts of predicted secondary structures of VdAS1 were ahelices and random coils. The study results established the foundation for the heterologous expression and functional analysis of VdAS1.

Key words: Vaccinium dunalianum, Arbutin synthase, Gene cloning, Bioinformatics analysis

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