Tapprich W E, Goss D J, Dahlberg A E
Section of Biochemistry, Brown University, Providence RI 02912.
Proc Natl Acad Sci U S A. 1989 Jul;86(13):4927-31. doi: 10.1073/pnas.86.13.4927.
A single base was mutated from guanine to adenine at position 791 in 16S rRNA in the Escherichia coli rrnB operon on the multicopy plasmid pKK3535. The plasmid-coded rRNA was processed and assembled into 30S ribosomal subunits in E. coli and caused a retardation of cell growth. The mutation affected crucial functional roles of the 30S subunit in the initiation of protein synthesis. The affinity of the mutant 30S subunits for 50S subunits was reduced and the association equilibrium constant for initiation factor 3 was decreased by a factor of 10 compared to wild-type 30S subunits. The interrelationship among the region of residue 790 in 16S rRNA, subunit association, and initiation factor 3 binding during initiation complex formation, as revealed by this study, offers insights into the functional role of rRNA in protein synthesis.
在多拷贝质粒pKK3535上的大肠杆菌rrnB操纵子中,16S rRNA的第791位碱基由鸟嘌呤突变为腺嘌呤。质粒编码的rRNA在大肠杆菌中被加工并组装成30S核糖体亚基,导致细胞生长迟缓。该突变影响了30S亚基在蛋白质合成起始中的关键功能作用。与野生型30S亚基相比,突变型30S亚基与50S亚基的亲和力降低,起始因子3的缔合平衡常数降低了10倍。这项研究揭示了16S rRNA中790位残基区域、亚基缔合以及起始复合物形成过程中起始因子3结合之间的相互关系,为rRNA在蛋白质合成中的功能作用提供了见解。