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Cloning and bioinformatics analysis of cycloartenol synthase (HcCAS1) gene in Huperzia carinata / 中国中药杂志
China Journal of Chinese Materia Medica ; (24): 1715-1719, 2012.
Article in Chinese | WPRIM | ID: wpr-338775
ABSTRACT
<p><b>OBJECTIVE</b>To clone and sequence the open reading frame of cycloartenol synthase (CAS) from Huperzia carinata.</p><p><b>METHOD</b>After searching the transcriptome dataset of H. carinata, one unique sequence containing oxide squalene cyclases domain was discovered. The primers were designed according to the cDNA sequence of CAS from the dataset. And then, the open reading frame of CAS was cloned by RT-PCR strategy with the template of mixed RNA extracted from root, stem and leaf of H. carinata. The bioinformatic analysis of this gene and its corresponding protein was performed.</p><p><b>RESULT</b>One unique sequence of CAS, named as HcCAS1 (GenBank accession number JN790125) , was cloned from H. carinata. The open reading frame of HcCAS1 consists of 2 474 bp, encoding one polypeptide with 757 amino acids.</p><p><b>CONCLUSION</b>This study cloned and analyzed CAS from H. carinata for the first time. The result will provide a foundation for exploring the mechanism of sterol biosynthesis in Huperziaceae plants.</p>
Subject(s)
Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Molecular Sequence Data / Models, Molecular / Chemistry / Amino Acid Sequence / Cloning, Molecular / Protein Structure, Secondary / Evolution, Molecular / Computational Biology / Intramolecular Transferases Language: Chinese Journal: China Journal of Chinese Materia Medica Year: 2012 Type: Article

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Full text: Available Index: WPRIM (Western Pacific) Main subject: Phylogeny / Molecular Sequence Data / Models, Molecular / Chemistry / Amino Acid Sequence / Cloning, Molecular / Protein Structure, Secondary / Evolution, Molecular / Computational Biology / Intramolecular Transferases Language: Chinese Journal: China Journal of Chinese Materia Medica Year: 2012 Type: Article