Bringaud F, Peris M, Zen K H, Simpson L
Howard Hughes Medical Institute, University of California Los Angeles 90024, USA.
Mol Biochem Parasitol. 1995 Apr;71(1):65-79. doi: 10.1016/0166-6851(95)00023-t.
Two mitochondrial proteins with molecular masses of 18 and 51 kDa were isolated from Leishmania tarentolae, and N-terminal amino-acid sequences were obtained. The cDNAs and genes encoding these proteins were cloned using RT-PCR. The proteins were identified as components of the previously characterized mitochondrial ribonucleoprotein complexes, T-Ia and T-VI, by comigration in native gels. The p18 and p51 genes contain 17 and 9-amino-acid N-terminal sequences, which are not present in the mature proteins and may represent cleavable mitochondrial targeting sequences. There are two identical p18 genes separated by 1.7 kb in tandem array and both are transcribed. The p18 amino-acid sequence is not similar to any sequence in the database. Antiserum to p18 expressed in Escherichia coli reacts with the entire tubular mitochondrion. The p51 gene is single copy, and the amino-acid sequence is similar to mitochondrial aldehyde dehydrogenases from other organisms. The N-terminal amino-acid sequences of 71 and 62-kDa mitochondrial proteins which co-migrated in native gels with several other T-complexes were also obtained. The p71 sequence proved to be similar to hsp70 sequences from other organisms. The p62 sequence was identical to an hsp60 sequence from Trypanosoma brucei.
从热带利什曼原虫中分离出两种分子量分别为18 kDa和51 kDa的线粒体蛋白，并获得了其N端氨基酸序列。使用逆转录聚合酶链反应（RT-PCR）克隆了编码这些蛋白的cDNA和基因。通过在天然凝胶中的共迁移，这些蛋白被鉴定为先前表征的线粒体核糖核蛋白复合物T-Ia和T-VI的组成部分。p18和p51基因包含17个和9个氨基酸的N端序列，这些序列在成熟蛋白中不存在，可能代表可裂解的线粒体靶向序列。有两个相同的p18基因以串联排列的方式相隔1.7 kb，并且都被转录。p18氨基酸序列与数据库中的任何序列都不相似。在大肠杆菌中表达的针对p18的抗血清与整个管状线粒体发生反应。p51基因是单拷贝的，其氨基酸序列与其他生物的线粒体醛脱氢酶相似。还获得了在天然凝胶中与其他几种T复合物共迁移的71 kDa和62 kDa线粒体蛋白的N端氨基酸序列。p71序列被证明与其他生物的热休克蛋白70（hsp70）序列相似。p62序列与布氏锥虫的热休克蛋白60（hsp60）序列相同。
