中文摘要：

[目的]基于生物信息学方法分析人线粒体转录延伸因子TEFM蛋白的结构和功能。[方法]检索Uniprot数据库中人线粒体转录终止因子TEFM蛋白的氨基酸序列，利用生物信息学方法对人TEFM的理化性质、物种间的蛋白质同源性、跨膜区、亲水性／疏水性、亚细胞定位、蛋白质二级结构、保守结构域、蛋白质三级结构、蛋白质相互作用进行预测与分析。[结果]人TEFM全长360个氨基酸，理论等电点9．39，属于TEFM蛋白超家族，不含跨膜区，属于亲水蛋白；人TEFM含有一个保守的螺旋-发夹-螺旋（HHH_3）结构域，二级结构以α-螺旋和无规则卷曲为主，三维建模空间结构与二级结构预测结果相符，进一步分析建模结果可靠。与人TEFM相互作用的蛋白质均为线粒体DNA转录因子或线粒体RNA聚合酶。[结论]人TEFM具有线粒体转录延伸因子蛋白超家族的典型结构，生物信息学分析结果对深入研究人TEFM在线粒体基因转录调控中的作用具有一定的理论指导意义。

英文摘要：

[ Objective ] To analysis the structure and function of mitochondrial transcription elongation factor of Homo sapiens using bioinformatics methods. [ Methods] Based on the amino acid sequence of mitochondrial transcription elongation factor of Homo sapiens from Uniprot database, the bioinfonnatics analyses were performed, including protein physicochemical property, the phylogenetic tree of TEFM related proteins from different species, hydrophilicity/hydrophobicity, transmembrane region, sub- cellular localization, protein secondary structure, conserved domain, protein tertiary structure, as well as protein - protein inter- action. [ Results] Human TEFM protein consists of 360 amino acids,with theoretical isoelectric point of 9.62. This protein be- longs to the TEFM protein superfamily without transmembrane region, and it is a hydrophilic protein. Main composition of the human TEFM protein secondary structure wereα- helix and random coil. Human TEFM have a conserved helix - hairpin - halix （HHH_3） domain. The predicted three - dimensional structure of TEFM was similar with secondary stmcture prediction. Further analysis proved that the predicted protein structure was stable. It showed that the 6 most relevant interaction proteins with the TEFM protein were all mitochondrial transcription factors or mitochondrial RNA polymerase. [ Conclusion] Human TE- FM protein contained the typical structure of TEFM protein family, and the analysis results of human TEFM provided great in-formation about TEFM in regulation of mitochondrial transcription elongation process for further research.