McMahon G, Landau J V
Biochim Biophys Acta. 1983 Mar 10;739(2):244-8. doi: 10.1016/0167-4781(83)90035-0.
We have used the application of hydrostatic pressure to modify the misreading of polyuridylate template. Pressure was used to test ribosomes isolated from Escherichia coli strains containing mutations in the S12 ribosomal protein which lead to streptomycin-resistance and -dependence. The incorporation of phenylalanine into polypeptide, at a given pressure, was found to vary with the source of ribosomes and was found to correlate with S12-dependent changes in rates of incorporation suggesting a role of the S12 ribosomal protein in the pressure effect. Streptomycin partially alleviated the increased pressure-resistance in those cases where control rates of incorporation were found to be stimulated by the addition of streptomycin. In contrast, the misincorporation of isoleucine was substantially more sensitive to pressure application, regardless of ribosome source or the presence of streptomycin. These results suggest that the application of hydrostatic pressure affects at least two distinct ribosomal reactions important to the discrimination of these two amino acids.
我们利用流体静压力来改变聚尿苷酸模板的错读。压力被用于测试从含有核糖体蛋白S12突变的大肠杆菌菌株中分离出的核糖体，这些突变导致对链霉素耐药和依赖。在给定压力下，发现苯丙氨酸掺入多肽的情况随核糖体来源而变化，并且发现与掺入速率中S12依赖性变化相关，这表明核糖体蛋白S12在压力效应中起作用。在那些发现添加链霉素能刺激掺入对照速率的情况下，链霉素部分缓解了增加的压力抗性。相比之下，异亮氨酸的错误掺入对施加压力更为敏感，无论核糖体来源或链霉素的存在与否。这些结果表明，流体静压力的施加影响了至少两个对这两种氨基酸区分很重要的不同核糖体反应。
