Hummel H, Piepersberg W, Böck A
Mol Gen Genet. 1980;179(1):147-53. doi: 10.1007/BF00268457.
Mutants were analyzed biochemically and genetically in which restriction of translational misreading by ribosomes containing an altered L6 protein is relieved. Amongst 100 such strains eight possessed an altered S4 and two a mutant S5 protein. The protein-chemical type of L6 mutation seems to influence the kind of S4 mutant form selected. Also, only a few types of S4 ram mutations are obtained and they are different from those usually found amongst suppressors of streptomycin-dependent (SmD) strains. The S4 mutations selected are able to reduce the level of streptomycin-resistance of strA1 or strA40 strains and they confer extreme hypersensitivity to aminoglycosides when present alone. On the other hand, S4 mutations from SmD suppressor strains only weakly reverse L6 restriction. The results imply that control of translational fidelity is an intersubunit function and that protein L6 (an interface protein) cooperates with 30S proteins by directly or indirectly determining parameters involved in aminoacyl-tRNA recognition.
对含有改变的L6蛋白的核糖体对翻译错读的限制得到缓解的突变体进行了生化和遗传学分析。在100个这样的菌株中，有8个具有改变的S4，2个具有突变的S5蛋白。L6突变的蛋白质化学类型似乎影响所选择的S4突变形式的种类。此外，只获得了几种类型的S4 ram突变，它们与通常在链霉素依赖（SmD）菌株的抑制子中发现的突变不同。所选择的S4突变能够降低strA1或strA40菌株的链霉素抗性水平，并且当单独存在时，它们对氨基糖苷类药物表现出极端的超敏感性。另一方面，来自SmD抑制子菌株的S4突变只能微弱地逆转L6限制。结果表明，翻译保真度的控制是亚基间的功能，并且蛋白质L6（一种界面蛋白）通过直接或间接确定参与氨酰-tRNA识别的参数与30S蛋白协同作用。
