Identification and Analysis of Muscle-Related Protein Isoforms Expressed in the White Muscle of the Mandarin Fish (Siniperca chuatsi)

被引:0
|
作者
Guoqiang Zhang
Wuying Chu
Songnian Hu
Tao Meng
Linlin Pan
Renxue Zhou
Zhen Liu
Jianshe Zhang
机构
[1] Changsha University,Department of Bioengineering & Environmental Science
[2] Chinese Academy of Sciences,Key Laboratory of Genome Information and Sciences, Beijing Institute of Genomics
[3] Graduated University of the Chinese Academy of Sciences,undefined
来源
Marine Biotechnology | 2011年 / 13卷
关键词
Mandarin fish; ESTs; White muscle; Muscle protein; Isoforms;
D O I
暂无
中图分类号
学科分类号
摘要
To identify muscle-related protein isoforms expressed in the white muscle of the mandarin fish Siniperca chuatsi, we analyzed 5,063 high-quality expressed sequence tags (ESTs) from white muscle cDNA library and predicted the integrity of the clusters annotated to these genes and the physiochemical properties of the putative polypeptides with full length. Up to about 33% of total ESTs were annotated to muscle-related proteins: myosin, actin, tropomyosin/troponin complex, parvalbumin, and Sarcoplasmic/endoplasmic reticulum calcium ATPase (SERCa). Thirty-two isoforms were identified and more than one isoform existed in each of these proteins. Among these isoforms, 14 putative polypeptides were with full length. In addition, about 2% of total ESTs were significantly homologous to “glue” molecules such as alpha-actinins, myosin-binding proteins, myomesin, tropomodulin, cofilin, profilin, twinfilins, coronin-1, and nebulin, which were required for the integrity and maintenance of the muscle sarcomere. The results demonstrated that multiple isoforms of major muscle-related proteins were expressed in S. chuatsi white muscle. The analysis on these isoforms and other proteins sequences will greatly aid our systematic understanding of the high flexibility of mandarin fish white muscle at molecular level and expand the utility of fish systems as models for the muscle genetic control and function.
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页码:151 / 162
页数:11
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