Subramanian A R, Mizushima S
J Biol Chem. 1979 Jun 10;254(11):4309-12.
An altered form of ribosomal protein S1 from a mutant of Escherichia coli has been isolated and characterized. The mutant protein (denoted m1-S1) has a molecular weight of 57,000 as shown by sodium dodecyl sulfate-gel electrophoresis and the same NH2-terminal sequence as wild type S1. Protein m1-S1 binds poly(U) in the same manner as protein S1 and is active in protein synthesis with either synthetic or natural mRNA. Thus, about 75% of the sequence of protein S1 (which includes the NH2-terminal region) contains essentially all the functional domains of this protein involved in protein biosynthesis.
已从大肠杆菌突变体中分离并鉴定出核糖体蛋白S1的一种变体形式。如十二烷基硫酸钠-凝胶电泳所示,突变蛋白(称为m1-S1)的分子量为57,000,并且与野生型S1具有相同的NH2末端序列。蛋白m1-S1与蛋白S1以相同方式结合聚尿苷酸(poly(U)),并且在使用合成或天然mRNA的蛋白质合成中具有活性。因此,蛋白S1约75%的序列(包括NH2末端区域)基本上包含了该蛋白参与蛋白质生物合成的所有功能域。