Linxia Zhao

Publications (2)2.77 Total impact

• Source

  Available from: jbmb.or.kr

  Article: Molecular cloning and characterization of a new cDNA encoding hyoscyamine 6beta-hydroxylase from roots of Anisodus acutangulus.

  Guoyin Kai, Junfeng Chen, Li Li, Genyu Zhou, Limin Zhou, Lei Zhang, Yuhui Chen, Linxia Zhao
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  ABSTRACT: A new full-length cDNA encoding hyoscyamine 6beta-hydroxylase (designated as aah6h, GenBank Accession No. EF187826), which catalyzes the last committed step in the scopolamine biosynthetic pathway, was isolated from young roots of Anisodus acutangulus by rapid amplification of cDNA ends (RACE) for the first time. The full-length cDNA of aah6h was 1380 bp and contained a 1035 bp open reading frame (ORF) encoding a deduced protein of 344 amino acid residues. The deduced protein had an isoelectric point (pI) of 5.09 and a calculated molecular mass of about 38.7 kDa. Sequence analyses showed that AaH6H had high homology with other H6Hs isolated from some scopolamine-producing plants such as Hyoscyamus niger, Datura metel and Atropa belladonna etc. Bioinformatics analyses results indicated AaH6H belongs to 2-oxoglutarate-dependent dioxygenase superfamily. Phylogenetic tree analysis showed that AaH6H had closest relationship with H6H from A. tanguticus. Southern hybridization analysis of the genomic DNA revealed that aah6h belonged to a multi-copy gene family. Tissue expression pattern analysis firstly founded that aah6h expressed in all the tested tissues including roots, stems and leaves and indicated that aah6h was a constitutive-expression gene, which was the first reported tissue-independent h6h gene compared to other known h6h genes.
  Journal of biochemistry and molecular biology 10/2007; 40(5):715-22. · 2.02 Impact Factor
• Article: Molecular cloning of a new lectin gene from Z. grandiflora.

  Guoyin Kai, Jingui Zheng, Lei Zhang, Yongzhen Pang, Zhihua Liao, Zhugang Li, Linxia Zhao, Xiaofen Sun, Kexuan Tang
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  ABSTRACT: Using RNA extracted from Zephyrathes grandiflora young leaves and primers designed according to the conservative regions of Amaryllidaceae lectins, the full-length cDNA of Z. grandiflora agglutinin (ZGA) was cloned by rapid amplification of cDNA ends (RACE). The full-length cDNA of ZGA was 934 bp and contained a 576 bp open reading frame (ORF) encoding a 191 amino acid protein. Through comparative analysis of zga gene and its deduced amino acid sequence with those of other Amaryllidaceae species, it was found that zga encoded a precursor lectin with signal peptide. Molecular modeling suggested that ZGA was a mannose-binding lectin with three mannose-binding sites like lectins from other Amaryllidaceae species. Southern blot analysis of the genomic DNA revealed that zga belonged to a multi-copy gene family like those of many other Amaryllidaceae species such as Galanthus nivalis and Clivia miniata.
  DNA Sequence 09/2003; 14(4):335-8. · 0.75 Impact Factor