Beauchamp P M, Horn E W, Gross S R
Proc Natl Acad Sci U S A. 1977 Mar;74(3):1172-6. doi: 10.1073/pnas.74.3.1172.
Genetic analysis of an electrophoretic variant of the mitochondrial leucyl-tRNA synthetase [L-leucine:tRNALeu ligase (AMP-forming), EC 6.1.1.4] indicates that it is either an allele of or linked closely to leu-5ts, a mutant that is known to produce a cytoplasmic leucyl-tRNA synthetase with an altered affinity for leucine as well as being deficient in the production of the mitochondrial enzyme. Immunological analysis indicates that the two synthetases have little, if any, structural homology. The pattern of synthesis of the enzymes in leu-5ts revertants, the reciprocal relationship of the production of the two enzymes in response to a negative regulatory element, presumably of mitochondrial origin, as well as the lack of detectable structural homology, led to the proposal that the phenotype of leu-5ts results from a mutational alteration in the structural gene for the cytoplasmic enzyme in a region involved in the initiation of transcription of the adjacent gene for the mitochondrial enzyme.
对线粒体亮氨酰 - tRNA合成酶[L - 亮氨酸:tRNALeu连接酶(AMP形成), EC 6.1.1.4]的一种电泳变体进行遗传分析表明,它要么是leu - 5ts的等位基因,要么与leu - 5ts紧密连锁,leu - 5ts是一种已知会产生对亮氨酸亲和力改变的细胞质亮氨酰 - tRNA合成酶且线粒体酶产生不足的突变体。免疫分析表明这两种合成酶几乎没有结构同源性(如果有的话)。leu - 5ts回复体中酶的合成模式、两种酶的产生对可能源自线粒体的负调控元件的相互关系,以及缺乏可检测到的结构同源性,导致有人提出leu - 5ts的表型是由于细胞质酶结构基因中与线粒体酶相邻基因转录起始相关区域的突变改变所致。