人线粒体转录终止因子1（hMTERF1）蛋白的生物信息学分析

摘要

To study the structure and biological function of the human mitochondrial transcription termination factor 1 ( hMTERF1 ) . Many bioinformatics methods were used to analysis physical and chemical properties, hydrophobicity, transmembrane region, signal peptide, secondary structure, functional domain and assortment, multiple alignment, phylogenetic tree and three⁃dimensional structures of hMTERF1. The results showed that hMTERF1 was hydrophilic protein and the calculated molecular mass was 45.78 kD and the theoretical isoelectric point was 9.49. No signal peptide and transmembrane regions were found in the protein. hMTERF1 was localized in human mitochodria, and the N⁃terminal 1~57 amino acids were transit peptide. Main composition of the protein secondary structure were a⁃helix and random coil, and it contains 6 MTERF motif. The three⁃demensional structure prediction showed similar results with secondary structure prediction. The multiple alignment and clustering analysis showed that hMTERF1 is an orthologous protein belong to MTERF family, and has high similarity to Pongo pygmaeus, Rattus norvegicus, and Mus musculus MTERF1. The bioinformatic analysis will be helpful for the further study of the function of hMTERF1.%为了预测和分析人线粒体转录终止因子1（ human mitochondrial transcription termination factor 1， hMTERF1）蛋白的结构与功能。采用生物信息学的方法对hMTERF1进行系统的分析与研究，包括hMTERF1的理化性质、跨膜区和信号肽、亚细胞定位、二级结构功能域、蛋白质的功能分类预测、多重序列比对与系统发育树构建、三级结构建模。结果表明：hMTERF1蛋白分子量为45．78 kD，等电点为9．49，不具有信号肽和跨膜区。该蛋白定位于细胞线粒体，N端1～57个氨基酸为前导肽序列。其二级结构主要为a螺旋和无规则卷曲，包含6个MTERF基序，三级结构显示结果与二级结构预测结果相符。蛋白质多重序列比对和聚类分析显示，hMTERF1蛋白与黑猩猩、大鼠、小鼠等哺乳动物的MTERF1蛋白具有高度同源性，在系统发育树上聚为一簇。 hMTERF1的生物信息学分析为进一步探索hMTERF1蛋白的功能提供参考资料和理论依据。