›› 2010, Vol. 53 ›› Issue (5): 587-595.doi:

• 研究论文 • 上一篇    下一篇

拟黑多刺蚁雌激素相关受体基因cDNA的克隆及生物信息学分析

欧阳霞辉,赵有红,侯兰新,奚耕思   

  • 出版日期:2010-05-20 发布日期:2010-05-20
  • 通讯作者: 欧阳霞辉

Cloning and bioinformatic analysis of cDNA of estrogen related receptor gene from Polyrhachis vicina Roger (Hymenoptera: Formicidae)

OUYANG Xia-hu, ZHAO You-Hong, HOU Lan-Xin, XI Geng-Si   

  • Online:2010-05-20 Published:2010-05-20

摘要: 雌激素相关受体(estrogen related receptors, ERRs)能够直接与类固醇激素受体共激活子(steroidhormone receptor coactivator,SRC)结合,激活靶基因的表达,与众多生理和发育过程有关.采用RT-PCR、RACE等方法从拟黑多刺蚁Polyrhachis vicina Roger克隆得到了雌激素相关受体基因的cDNA克隆,命名为pvERR  (GenBank 登录号为EF474463),并采用生物信息学方法对其cDNA和编码的蛋白质的理化性质、蛋白质二级及三级结构、分子系统进化关系等进行了预测和推断.结果表明:pvERR基因cDNA全长1 935 bp,包含一个1 305 bp的开放阅读框、245 bp的5′-UTR 和385 bp的3′-UTR,编码一个由434个氨基酸组成的蛋白质.pvERR的配体结合区(ligand binding domain,LBD)主要由两个β折叠和11个α螺旋(H1, H3~H12, 缺少H2)构成,这与哺乳类动物已知晶体结构的ERRγ的配体结合区结构非常相似.pvERR氨基酸序列与其他昆虫ERRs氨基酸序列同源性很高,它与西方蜜蜂Apis mellifera雌激素相关受体amERR氨基酸序列相似性达到89.9 %;在进化关系上,pvERR与人类Homo sapiens ERRs的关系比果蝇Drosophila melanogaster雌激素相关受体dERR与人类的更近.本文可为进一步研究pvERR在昆虫发育中的功能提供有价值的信息.

关键词: 拟黑多刺蚁, pvERR, 分子克隆, 生物信息学分析, 蛋白质结构预测

Abstract: Estrogen related receptor (ERR) can bind to the member of steroid receptor co-activator family and activate transcription activity of the target genes. ERRs have been found to be present in many animal species and play important roles in regulation of many physiological processes. A full-length cDNA of the ERR gene, named pvERR (GenBank accession no. EF474463), was cloned from Polyrhachis vicina Roger by using RT-PCR and RACE methods. The nucleotide sequence and deduced amino acid sequences of pvERR were analyzed and characterized by bioinformatic methods. The results showed that the full-length cDNA of pvERR gene is 1 918 bp, containing an open reading frame of 1 305 bp, 5′-UTR of 245 bp and 3′-UTR of 368 bp. The cDNA encoded a protein with 434 amino acids. The ligand-binding domain (LBD) of pvERRs consists of two β-sheets and eleven α-helixs (H1, H3-H12, lack of H2) and the LBD structure is similar to that of mammalian ERRγ, whose crystal-structure is known. The homology analysis suggests that the pvERR and the amERR proteins share 89.9% identities in their amino acid sequences, and the homology between them is the highest in all known insect ERRs; phylogenetic relationgship between pvERR and human ERRs is closer than that between Drosophila dERR and human ERRs. This study may provide valuable information for further research on pvERR.

Key words: Polyrhachis vicina, pvERR, molecular cloning, bioinformatic analysis, protein structure prediction