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首页> 外文期刊>Molecular and Cellular Biology >Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen.
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Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen.

机译:人线粒体蛋白的一级结构,与细菌和植物伴侣蛋白以及65千达尔顿分枝杆菌抗原同源。

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摘要

The complete cDNA for a human mitochondrial protein designated P1, which was previously identified as a microtubule-related protein, has been cloned and sequenced. The deduced amino acid sequence of P1 shows strong homology (40 to 50% identical residues and an additional 20% conservative replacements) to the 65-kilodalton major antigen of mycobacteria, to the GroEL protein of Escherichia coli, and to the ribulose 1,5-bisphosphate carboxylase-oxygenase (rubisco) subunit binding protein of plant chloroplasts. Similar to the case with the latter two proteins, which have been shown to act as chaperonins in the posttranslational assembly of oligomeric protein structures, it is suggested that P1 may play a similar role in mammalian cells. The observed high degree of homology between human P1 and mycobacterial antigen also suggests the possible involvement of this protein in certain autoimmune diseases.
机译:已经克隆并测序了人类线粒体蛋白P1的完整cDNA,该蛋白先前已被鉴定为微管相关蛋白。推导的P1氨基酸序列与分枝杆菌的65千达尔顿主要抗原,大肠杆菌的GroEL蛋白以及核糖1,5具有强同源性(40至50%相同残基,另外20%保守取代)。 -叶绿体中的-双磷酸羧化酶加氧酶(rubisco)亚基结合蛋白。与后两种蛋白质的情况相似(已显示它们在寡聚蛋白质结构的翻译后组装中充当伴侣蛋白),这表明P1在哺乳动物细胞中可能起类似的作用。观察到的人P1和分枝杆菌抗原之间的高度同源性也表明该蛋白可能与某些自身免疫性疾病有关。

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