研究报告

人类(Homo sapiens)肌肉增强因子2(MEF2)生物信息学特性比较及其进化分析

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  • 西安文理学院生命科学系, 西安 710065

收稿日期: 2010-11-28

  修回日期: 2011-01-28

  网络出版日期: 2011-09-25

Properties comparing and evolutionary analysis of MEF2 of Homo sapiens based on bioinformatic methods

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  • Department of Life Science, Xi’an University of Arts and Science, Xi’an 710065, China

Received date: 2010-11-28

  Revised date: 2011-01-28

  Online published: 2011-09-25

摘要

肌肉增强因子2(Myocyte enhancer factor 2, MEF2)是MADS(MCM1, agamous, deficiens和serum response factor)家族成员之一, 在动物发育过程中起到重要的调节作用。为了进一步了解其调控的复杂性, 本文根据NCBI中已有的人类MEF2相关数据, 应用ExPASy在线序列分析工具、CBS在线分析服务器软件、Conserved Domain Database(CDD)数据库、SABLE在线分析软件等对人类MEF2蛋白的不同亚型序列进行比较分析, 同时, 根据相关序列的比对结果构建系统进化树进行分析。结果表明, MEF2在人体内以多种蛋白形式存在, 其理化性质存在一定差别, 可能的翻译后糖基化修饰多为O型糖基化且均存在较多磷酸化位点。人类各MEF2蛋白具明显MADS结构域, 多数具有MEF2结构域和HJURP_C结构域。各MEF2蛋白二级结构均包括了螺旋、折叠和无规则卷曲等多种形式, 其三级结构模式相似。系统进化树显示MEF2B蛋白与其他蛋白有着较大的序列差异及较远进化关系, 可能较为原始。

本文引用格式

郭新军 . 人类(Homo sapiens)肌肉增强因子2(MEF2)生物信息学特性比较及其进化分析[J]. 遗传, 2011 , 33(9) : 975 -981 . DOI: 10.3724/SP.J.1005.2011.00975

Abstract

As one of the members of MADS family, MEF2 group is important in regulating development. Analytical tools of NCBI, ExPASy, CBS, CDD, and SABLE were adopted to analyze the properties of human MEF2 proteins, and evolutionary tree was built according to the result of correlative sequence alignments. The results showed that there are various forms of MEF2 in human body, and there are some differences in the physicochemical characteristics. Relatively more phosphorylation sites are found and the main glycosylation sites are N-glycosylation sites. All MEF2 proteins of human contain MADS domain, and most contain MEF2 domain and HJURP_C domain. Their secondary structures contain three dominant states: helix, sheet and coil, their tertiary structures are similar. The phylogenetic tree result shows that MEF2B may be original because of its difference of sequences and evolutional relation.

参考文献

[1] Lyons GE, Micales BK, Schwarz J, Martin JF, Olson EN. Expression of Mef2 genes in the mouse central nervous system suggests a role in neuronal maturation. J Neurosci, 1995, 15(8): 5727-5738.
[2] Breitbart RE, Liang CS, Smoot LB, Laheru DA, Mahdavi V, Nadal-Ginard B. A fourth human MEF2 transcription factor, hMEF2D, is an early marker of the myogenic lineage. Development, 1993, 118(4): 1095-1106.
[3] 张颖, 王利凤, 邵明, 张红卫. 文昌鱼AmphiMef2基因的特征及其发育表达. 中国科学(C辑: 生命科学), 2007, 37(4): 422-426.
[4] Chambers AE, Kotecha S, Towers N, Mohun TJ. Muscle-specific expression of SRF-related genes in the early embryo of Xenopus laevis. EMBO J, 1992, 11(13): 4981-4991.
[5] Ticho BS, Stainier DYR, Fishman MC, Breitbart RE. Three zebrafish Mef2 genes delineate somitic and cardiac muscle development in wild-type and mutant embryos. Mech Dev, 1996, 59(2): 205-218.
[6] Gossett LA, Kelvin DJ, Sternberg EA, Olson EN. A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes. Mol Cell Biol, 1989, 9(11): 5022-5033.
[7] 程震龙, 朱大海, 张志谦. MEF2与肌肉发生. 遗传, 2002, 24(5): 581-585.
[8] Cripps RM, Black BL, Zhao B, Lien CL, Schulz RA, Olson EN. The myogenic regulatory gene Mef2 is a direct target for transcriptional activation by Twist during Drosophila myogenesis. Genes Dev, 1998, 12(3): 422-434.
[9] Shalizi A, Bonni A. Not just for muscle anymore: activity and calcium regulation of MEF2-dependent transcription in neuronal survival and differentiation. In: Dudek SM, ed. Transcriptional Regulation by Neuronal Activity. New York: Springer, 2008: 229-250.
[10] Kim MK, Kim SC, Kang JI, Hyun JH, Boo HJ, Eun SY, Park DB, Yoo ES, Kang HK, Kang JH. 6-Hydroxydopamine-induced PC12 cell death is mediated by MEF2D down-regulation. Neurochem Res, 2011, 36(2): 223-231.
[11] Pereira AHM, Clemente CFMZ, Cardoso AC, Theizen TH, Rocco SA, Judice CC, Guido MC, Pascoal VDB, Lopes-Cendes I, Souza JRM, Franchini KG. MEF2C silencing attenuates load-induced left ventricular hypertrophy by modulating mTOR/S6K pathway in mice. PLoS One, 2009, 4(12): e8472.
[12] Gasteiger E, Hoogland C, Gattiker A, Duvaud S, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. In: Walker JM, ed. The Proteomics Pro-tocols Handbook. Totowa: Humana Press, 2005: 571-607.
[13] Blom N, Gammeltoft S, Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol, 1999, 294(5): 1351-1362.
[14] Julenius K, Mølgaard A, Gupta R, Brunak S. Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology, 2005, 15(2): 153-164.
[15] Marchler-Bauer A, Anderson JB, Chitsaz F, Derbyshire MK, DeWeese-Scott C, Fong JH, Geer LY, Geer RC, Gonzales NR, Gwadz M, He SQ, Hurwitz DI, Jackson JD, Ke ZX, Lanczycki CJ, Liebert CA, Liu CL, Lu F, Lu SN, Marchler GH, Mullokandov M, Song JS, Tasneem A, Thanki N, Yamashita RA, Zhang DC, Zhang NG, Bryant SH. CDD: specific functional annotation with the Conserved Domain Database. Nucleic Acids Res, 2009, 37(Suppl.1): D205-D210.
[16] Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics, 2006, 22(2): 195-201.
[17] Kumar S, Dudley J, Nei M, Tamura K. MEGA: A biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinform, 2008, 9(4): 299-306.
[18] Tamura K, Dudley J, Nei M, Kumar S. MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol, 2007, 24(8): 1596-1599.
[19] Zuckerkandl E, Pauling L. Evolutionary divergence and convergence in proteins. In: Bryson V, Vogel HJ, eds. Evol
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