Inhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.

Proceedings of the National Academy of Sciences of the United States of America

PubMedID: 4551985

Cabrer B, Vázquez D, Modolell J. Inhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes. Proc Natl Acad Sci USA. 1972;69(3):733-6.
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.