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草业学报 ›› 2013, Vol. 22 ›› Issue (5): 96-103.DOI: 10.11686/cyxb20130511

• 研究论文 • 上一篇    下一篇

中国荷斯坦奶牛铁蛋白基因3′端克隆及序列分析

罗佳捷1,彭瑛3,罗锐1,张彬1*,李丽立2*,吴力专1,占今舜1,邢月腾1   

  1. 1.湖南农业大学动物科学技术学院,湖南 长沙 410128;
    2.中国科学院亚热带农业生态研究所 动物生态营养与健康养殖联合实验室 农业生态工程重点实验室,湖南 长沙 410125;
    3.湖南广播电视大学农医部,湖南 长沙 410004
  • 出版日期:2013-10-20 发布日期:2013-10-20
  • 通讯作者: E-mail:zhb8236@126.com, lili@isa.ac.cn
  • 作者简介:罗佳捷(1984-),男,湖南湘潭人,在读博士。
  • 基金资助:
    国家自然科学基金项目(31072053;30671516),教育部高等学校博士学科点专项科研基金(博导类)项目(20104320110001),湖南省自然科学基金重点项目(11JJ2014)和湖南省博士生科技创新项目(CX2010B284)资助。

3′ end cloning and sequence analysis of the FTH gene from Chinese Holstein cattle

LUO Jia-jie1, PENG Ying3, LUO Rui1, ZHANG Bin1, LI Li-li2, WU Li-zhuan1, ZHAN Jin-shun1, XING Yue-teng1   

  1. 1.College of Animal Science and Technology, Hunan Agricultural University, Changsha 410128, China;
    2.Laboratory of Animal Nutrition and Human Health and Key Laboratory of Agro-ecology, Institute of Subtropical Agriculture, the Chinese Academy of Sciences, Changsha 410125, China;
    3.Faculty of Agriculture and Medicine, Hunan Radio and TV University, Changsha 410004, China
  • Online:2013-10-20 Published:2013-10-20

摘要: 本研究旨在克隆和分析中国荷斯坦奶牛的铁蛋白(FTH)基因,为该基因的功能研究和有效利用提供理论依据。运用 cDNA 末端快速扩增(RACE)技术从公犊肝脏组织中扩增出FTH基因的3′端cDNA序列,并利用生物信息学方法对该基因的氨基酸序列进行分析。结果表明,FTH基因3′端cDNA全长为489 bp,编码81个氨基酸;经生物信息学分析表明,该基因编码的蛋白无N端信号肽及跨膜区,相对分子质量为9.125 3 kD,理论等电点为5.19,脂肪系数为85.56,总亲水性为-0.342,其一级结构中存在4个功能结构域;二级结构元件以α-螺旋和β-旋转为主;同源序列分析表明,中国荷斯坦奶牛与原牛FTH氨基酸的相似性最高(99%);系统进化树显示,在该基因座位上中国荷斯坦奶牛与所测物种的亲缘关系均较远。本研究有助于揭示FTH家族基因的进化历史,为对其进行深入的功能分析和利用研究提供参考。

Abstract: The 3′ end cDNA sequence and amino acid sequence of the FTH (ferritin) gene from Chinese Holstein cattle was cloned and analyzed to provide a theoretical basis for functional studies and its effective utilization. The 3′ end cDNA was cloned from liver tissues by rapid amplification of cDNA ends (RACE), and the bioinformatics method was used to analyze the amino acid sequence. The 3′ end cDNA of the FTH gene was 489 bp and it encoded a peptide of 81 amino acids. Its relative molecular weight was 9.125 3 kD, isoelectric point was 5.19, fat index was 85.56, grand average of hydropathy was -0.342. N-terminal signal peptides and transmembrane domains were not included in this protein. The primary structure of the FTH protein contained four functional domains, and the secondary structure was mainly an α-helix with β-rotation. The results obtained through homologous sequencing indicated that the FTH of Chinese Holstein cattle had a high similarity to that of Bos taurus (99%), and the molecular evolution trees showed that the FTH of Chinese Holstein cattle had very low genetic relationships with other species studied in this research. These results provided clues for evolutionary studies of the FTH gene family, as well as serving as references for further functional analysis and utilization.

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