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      https://www.ias.ac.in/article/fulltext/jbsc/030/02/0213-0220

    • Keywords

       

      Mannose-binding lectin; RACE; Zingiber officinale ; ZOA

    • Abstract

       

      Using RNA extracted fromZingiber officinale rhizomes and primers designed according to the conservative regions of monocot mannose-binding lectins, the full-length cDNA ofZ. officinale agglutinin (ZOA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA ofzoa was 746 bp and contained a 510 bp open reading frame (ORF) encoding a lectin precursor of 169 amino acids with a signal peptide. ZOA was a mannose-binding lectin with three typical mannose-binding sites (QDNY). Semi-quantitative RT-PCR analysis revealed thatzoa expressed in all the tested tissues ofZ. officinale including leaf, root and rhizome, suggesting it to be a constitutively expressing form. ZOA protein was successfully expressed inEscherichia coli with the molecular weight expected. To our knowledge, this is the first mannose-binding lectin cDNA cloned from the family Zingiberaceae. Our results demonstrate that monocot mannose-binding lectins also occur within the family Zingiberaceae

    • Author Affiliations

       

      Zhonghai Chen1 Guoyin Kai2 Xiaojun Liu1 Juan Lin1 Xiaofen Sun1 Kexuan Tang1 2

      1. State Key Laboratory of Genetic Engineering, School of Life Sciences, Morgan-Tan International Center for Life Sciences Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Fudan University, Shanghai - 200433, People’s Republic of China
      2. Plant Biotechnology Research Center, School of Agriculture and Biology, Fudan-SJTU-Nottingham Plant Biotechnology R&D Center, Shanghai Jiao Tong University, Shanghai - 200030, People’s Republic of China
    • Dates

       
  • Journal of Biosciences | News

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