Cabrer B, Vázquez D, Modolell J
Proc Natl Acad Sci U S A. 1972 Mar;69(3):733-6. doi: 10.1073/pnas.69.3.733.
Elongation factor G (EF G), bound to ribosomes either with GMPPCP or with fusidic acid and GDP, inhibits elongation factor Tu (EF Tu)-dependent binding of Phe-tRNA on the ribosome-poly(U) complex and binding of Ala-tRNA on the initiation complex formed with RNA from bacteriophage R17; GTP hydrolysis associated with Phe-tRNA binding is also inhibited. Moreover, nonenzymic binding of Phe-tRNA at high Mg(++) concentration is completely blocked by EF G. Thus, EF G appears to bind at a site that overlaps or interacts with the ribosomal A-site.
延伸因子G(EF G),与结合了鸟苷5'-(β,γ-亚甲基)三磷酸(GMPPCP)或结合了夫西地酸和鸟苷二磷酸(GDP)的核糖体结合时,会抑制延伸因子Tu(EF Tu)依赖的苯丙氨酰 - tRNA在核糖体 - 聚尿苷酸(poly(U))复合物上的结合,以及丙氨酰 - tRNA在与噬菌体R17的RNA形成的起始复合物上的结合;与苯丙氨酰 - tRNA结合相关的鸟苷三磷酸(GTP)水解也受到抑制。此外,在高镁离子(Mg(++))浓度下苯丙氨酰 - tRNA的非酶促结合被EF G完全阻断。因此,EF G似乎结合在与核糖体A位点重叠或相互作用的位点上。