Miller D L
Proc Natl Acad Sci U S A. 1972 Mar;69(3):752-5. doi: 10.1073/pnas.69.3.752.
The binding of elongation factor EF G to ribosomes inhibits the subsequent reaction of the ribosomes with the ternary complex aminoacyl-tRNA.EF Tu.GTP. Both the hydrolysis of GTP and the binding of aminoacyl-tRNA to ribosomes are nearly abolished by the previous binding of factor EF G to ribosomes in the presence of either fusidic acid plus either GTP or a nonhydrolyzable analog of GTP. The results suggest that each elongation factor binds to the same region on the ribosome. The GTPase activities of both factors EF G and EF Tu may be activated by interaction at the same ribosomal site, as has been previously suggested by others.
延伸因子EF G与核糖体的结合会抑制核糖体随后与三元复合物氨酰 - tRNA.EF Tu.GTP的反应。在存在夫西地酸加上GTP或GTP的非水解类似物的情况下,因子EF G先前与核糖体的结合几乎完全消除了GTP的水解以及氨酰 - tRNA与核糖体的结合。结果表明,每个延伸因子都结合到核糖体上的同一区域。正如其他人之前所提出的,因子EF G和EF Tu的GTP酶活性可能通过在同一核糖体位点的相互作用而被激活。