作　　者： ; ; ; ; ; ; ; (蒋谋炎）;

机构地区： 南昌大学生命科学与食品工程学院

出　　处： 《水生生物学报》 2014年第6期1002-1007,共6页

摘　　要： 研究首次获得淡水珍珠贝池蝶蚌(Hyriopsis schlegelii)的致雄性化基因feminization-1C亚型,即fem-1c基因,并进行全长克隆及序列分析。从转录组中Race-PCR扩增fem-1c基因全长cDNA序列,用生物信息学方法对fem-1c基因进行基因组结构分析、多序列同源性比较、跨膜区段、亲疏水性分析、功能结构域预测等。研究结果如下:该cDNA序列全长2328 bp,包含一个1869 bp的最大开放阅读框,编码622个氨基酸,经同源比对和进化树分析,fem-1基因c亚型编码的氨基酸与太平洋牡蛎的同源性最高,为79%;疏水性分析显示该蛋白为亲水性蛋白;二级结构预测发现该蛋白有大量的α螺旋和随机卷曲,形成9个锚蛋白重复序列(Ankyrin repeat,ANK),同时,三级结构预测中可以清楚的看到9个ANK模体,跟SMART预测的结构位点结果相近。从无脊椎动物到脊椎动物fem-1c基因的保守性表明它们有共同的起源,暗示这个基因家族在功能上具备保守性,推测池蝶蚌fem-1c基因可能具备与线虫fem-1基因在性别决定方面上相似的功能。 We first reported the masculinized feminization gene(fem-1c) in the freshwater pearl mussel Hyriopsis schlegelii,which was cloned by Race-PCR from gonad tissue.Gene structure,multiple sequence homology alignment,transmembrane region,hydrophilia and hydrophobic property,and functional domain prediction was further analyzed using bioinformatics approaches.The full length of fem-1c gene was 2328 bp that contained an open reading frame of 1869 bp encoding 622 amino acid residues.The corresponding protein was stable and hydrophilic.Multiple sequence homology alignment showed that the Fem-1c proteins from H.schlegelii and C.gigas shared the highest amino acid identity(79%).The secondary structure of fem-1c protein mainly contained α-helix and random coil forming 9 ankyrin repeat(ANK) motifs.We also found 9 ANK motifs clearly in tertiary structure prediction by SMART soft.The conservation of the fem-1c from invertebrates to vertebrates suggested that these genes have a common ancient origin and that they may play a conserved role in the functions of these organisms.These results suggest that fem-1c gene in Hyriopsis schlegelii may have the similar functions with nematode Caenorhabditis elegans in sex determination.

关 键 词： 池蝶蚌 基因 克隆 序列分析 结构预测

领　　域： [生物学]