Minks M A, Subramanian A R
Biochim Biophys Acta. 1978 Sep 27;520(2):331-41. doi: 10.1016/0005-2787(78)90231-9.
The isolation and characterization of two low molecular weight, growth cycle-reflecting proteins which are associated with Escherichia coli ribosomes is described. These proteins which show greatly enhanced stoichiometry in ribosomes derived from post-exponential cells, exhibit molecular weights of 16 600, and 11 700 on sodium dodecyl sulfate (SDS) gel electrophoresis. Both proteins are highly acidic, the larger being the most acidic protein associated with the ribosome. Their amino acid compositions are unique and distinguish them from all other ribosomal proteins. Neither of the proteins showed crossreaction with either anti-L7 or anti-S6 sera although their electrophoretic behavior resembles that of L7 and S6. During the purification we have also isolated small amounts of three low molecular weight proteins showing some immunological homology with L7/L12. The isolated proteins were found to be without effect on the in vitro translation of f2-RNA, indicating that these adaptive modifications of the ribosome do not seriously affect its intrinsic activity.
本文描述了与大肠杆菌核糖体相关的两种低分子量、反映生长周期的蛋白质的分离与特性。这些蛋白质在指数生长期后细胞来源的核糖体中化学计量显著增加,在十二烷基硫酸钠(SDS)凝胶电泳上显示分子量分别为16600和11700。这两种蛋白质都高度酸性,较大的那种是与核糖体相关的酸性最强的蛋白质。它们的氨基酸组成独特,与所有其他核糖体蛋白质不同。尽管这两种蛋白质的电泳行为与L7和S6相似,但它们与抗L7或抗S6血清均无交叉反应。在纯化过程中,我们还分离出了少量与L7/L12有一些免疫同源性的低分子量蛋白质。发现分离出的蛋白质对f2-RNA的体外翻译没有影响,这表明核糖体的这些适应性修饰不会严重影响其内在活性。