Yaguchi M, Wittmann H G, Cábezon T, De Wilde M, Villarroel R, Herzog A, Bollen A
Mol Gen Genet. 1975 Dec 23;142(1):35-43. doi: 10.1007/BF00268753.
Protein S5 and S12 were isolated from 30S ribosomal subunits of two E. coli mutants highly resistant to the antibiotic neamine, and of the parental strain. Proteinchemical analyses on these proteins led to the following results: a) In protein S5 the arginine residue in peptide T2 of the parental strain is replaced by glycine in one (nea 314) or serine in the other (nea 319) of the two mutants. b) In protein S12 The proline residue in peptide T15 of the parental strain is replaced by leucine in mutant nea 314 and by glutamine in mutant nea 319. Comparison of these results with those obtained in earlier studies on other mutants with altered ribosomal proteins revealed that the amino acid replacements in neamine resistant mutants and in "revertants" from streptomycin dependence occur at the same amino acid positions of proteins S5 and S12. Therefore it is likely that both types of mutants belong to the same class.
从对新霉素高度耐药的两株大肠杆菌突变体以及亲代菌株的30S核糖体亚基中分离出了蛋白质S5和S12。对这些蛋白质进行的蛋白质化学分析得出了以下结果：a）在蛋白质S5中，亲代菌株肽段T2中的精氨酸残基在两个突变体中的一个（nea 314）被甘氨酸取代，在另一个（nea 319）中被丝氨酸取代。b）在蛋白质S12中，亲代菌株肽段T15中的脯氨酸残基在突变体nea 314中被亮氨酸取代，在突变体nea 319中被谷氨酰胺取代。将这些结果与早期对核糖体蛋白发生改变的其他突变体的研究结果进行比较后发现，新霉素耐药突变体和链霉素依赖性“回复突变体”中的氨基酸替换发生在蛋白质S5和S12的相同氨基酸位置。因此，这两种类型的突变体很可能属于同一类别。
