Molecular Cloning and Characteristics Analysis of ghrelin Gene in Asian Swamp Eel(Monopterus albus)

作     者：Guoliang RUAN Kai LIAO Daiqin YANG Xuwen BING Guoliang RUAN;Kai LIAO;Daiqin YANG;Xuwen BING

作者机构：Engineering Research Center of Ecology and Agricultural Use of WetlandMinistry of Education/College of Animal ScienceYangtze UniversityJingzhou 434025China Key Laboratory of Freshwater Fisheries and Germplasm Resources UtilizationsMinistry of Agriculture/Freshwater FisheriesResearch CenterChinese Academy of Fisheries SciencesWuxi 214081China Hubei Collaborative Innovation Center for Freshwater A uacultureWuhan 430070China 

出 版 物：《Agricultural Science & Technology》 (农业科学与技术（英文版）)

年 卷 期：2016年第17卷第4期

页      面：769-774页

学科分类：0908[农学-水产] 09[农学] 

基　　金：Supported by Natural Science Foundation of Hubei Province(2013CFB393) Open Fund of Key Laboratory of Freshwater Fisheries and Germplasm Resources Utilizations,Ministry of Agriculture(KF201307) National Pillar Program of China(2013BAD20B06) Pillar Program of Hubei Province(2015BBA235) Program for Outstanding Young and Middle-aged Scientific Innovation Team in Colleges and Universities of Hubei Province(T201503) 

主　　题：Monopterus albus ghrelin gene Clone Molecular structure 

摘      要：Ghrelin is an important signaling molecule linking reproductive and energy metabolism. In this study, ghrelin gene of Monopterus albus was cloned. Its structure and function were analysized preliminarily. By Rapid Amplification of cDNA Ends(RACE) technique, full-length cDNA and DNA sequences of ghrelin gene were obtained. The full-length ghrelin cDNA(GenBank accession no. JX122807) was 552 bp long, containing a 115 bp 5 -untranslated region, a 324 bp open reading frame and a 113 bp 3 -untranslated region. The full-length ghrelin DNA was 1 323 bp, consisting of three introns and four exons. The exon/intron junction sequences conformed to the GT/AG rule. Three introns were 594, 84 and 93 bp in length, respectively; four exons were229, 78, 112 and 133 bp in length, respectively. The results of amino acid sequence analysis showed that the deduced propreghrelin sequence of M. albus contained a signal peptide(SP) consisting of 22 amino acid residues, a mature peptide(MP)consisting of 19 amino acid residues and a C-terminal amino acid residue. Among them, the third amino acid of MP was serine(Ser^3) as the site for N-acylation and N-deacetylation reactions; the C-terminal amino acid residue sequence might contain a peptide hormone obestatin, which is a physiological antagonist of mature Ghrelin peptide. The homology and phylogenic relationships analyses of amino acid sequences suggested that propreghrelin of M. albus had high similarity to those of several Perciformes fishes; the propreghrelins of M. albus, Perciformes and Heterosomata fishes were clustered into a subgroup. The high conservatism of the gene structure and the amino acid sequences indicated that Ghrelin exerts important physiological functions and plays similar physiological mechanisms in vertebrates.