Cooperative control of translation fidelity by ribosomal proteins in Escherichia coli. I. Properties of ribosomal mutants whose resistance to neamine is the cumulative effect of two distinct mutations.
Cooperative control of translation fidelity by ribosomal proteins in Escherichia coli. I. Properties of ribosomal mutants whose resistance to neamine is the cumulative effect of two distinct mutations.
复制标题
大肠杆菌中核糖体蛋白对翻译保真度的协同控制。
DOI：
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发表时间：
1975
期刊：
影响因子：
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通讯作者：
A. Bollen
中科院分区：
文献类型：
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作者：
M. de Wilde;T. Cabezón;R. Villarroel;A. Herzog;A. Bollen
大肠杆菌菌株KMBL-146的两个自发突变体选择的耐氨基糖苷类抗生素新霉胺显示琥珀抑制剂在体内的严重限制。从突变株纯化的核糖体表现出低新霉胺诱导的误读在体外和相关的抗生素链霉素的亲和力降低。生化分析表明，突变体各有两个修饰的30 S核糖体蛋白，S12和S5。与这些结果一致，遗传分析表明存在两个突变，这两个突变本身都不赋予对新霉胺的抗性;位于基因rpxL（蛋白S12的结构基因）中的突变赋予链霉素依赖性，但这种依赖性在位于基因rpxE（蛋白S5的结构基因）中的第二个突变的存在下被抑制。
Two spontaneous mutants of Escherichia coli strain KMBL-146 selected for resistance to the aminoglycoside antibiotic neamine show severe restriction of amber suppressors in vivo. Purified ribosomes from the mutant strains exhibit low neamine-induced misreading in vitro and a decreased affinity for the related antibiotic streptomycin. Biochemical analysis shows that the mutants each have two modified 30S ribosmal proteins, S12 and S5. In agreement with these results, genetic analysis shows that two mutations are present, neither of which confers resistance to neamine by itself; the mutation located in gene rpxL (the structural gene for protein S12) confers streptomycin dependence but this dependence is suppressed in the presence of the second mutation, located in gene rpxE (the structural gene for protein S5).