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Cloning and Bioinformatics Analysis of MyoG Gene in Jinghai Yellow Chicken

ZHANG Tao1,2, ZHANG Gen-xi1,2,WANG Jin-yu1,2, FAN Qing-can1,2, WANG Wen-hao1,2, WEI Yue1,2, CHEN Xue-sen1,2, TANG Ying1,2,WANG Yong-juan3   

  1. 1. College of Animal Science and Technology, Yangzhou University, Yangzhou 225009, China;2. Key Laboratory for Animal Genetics, Breeding, Reproduction and Molecular Design of Jiangsu Province, Yangzhou 225009, China;3. Jiangsu Jinghai Poultry Group Co., Ltd., Nantong 226103, China
  • Received:2014-01-07 Online:2014-08-20 Published:2014-08-22

Abstract: Based on the published mRNA nucleotide sequence of Gallus gallus myogenin(MyoG) gene, a pair of primers were designed to clone the MyoG gene coding sequence of Jinghai Yellow chicken by RT-PCR. A variety of software and online tools were used for bioinformatic analysis of MyoG gene. Bioinformatics technology was successfully used to analyze the MyoG homology among different species, physical and chemical properties of the protein, transmembrane region of MyoG sequence, subcellular localization, hydrophilic, potential phosphorylation locus, conserved domain database, MyoG secondary structure and teriary structure. Finally, a 754 bp gene sequence was cloned, which contained CDS region, promoter region and part of the 3 ′region. Bioinformatics analysis showed that MyoG gene of Jinghai Yellow chicken was less conservative and shared 99.7%, 94.4%, 92.0%, 70.0%, 70.0%, 73.3%, 69.0%, 67.9%, 67.8% and 73.5% identity with Gallus gallus, Meleagris gallopavo, quail, horse, people, wild boar, cattle, goats, rats and sheep. The amino acid sequence analysis revealed that the MyoG gene of Jinghai Yellow chicken encoded water-soluble protein and its molecular weight was 25854 u, isoelectric point was 5.46, and did not belong to the membrane protein. Subcellular localization of MyoG was in the cytoplasm and it did not belong to the secreted protein. The MyoG protein contained six phosphorylation sites,a alkaline sequences, a HLH sequence, a low complexity sequence. The secondary structure of MyoG was mainly composed of random coil. The tertiary structure of domain area of MyoG protein showed a helix structure. The results above laid the foundation for further studies of expression regulation mechanism and function of MyoG gene in the muscle growth process.

Key words: Jinghai Yellow chicken; myogenin; cloning; bioinformatics analysis