Inhibition by elongation factor EF G of aminoacyl-tRNA binding to ribosomes.
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.
D000596:Amino Acids / Q000378:metabolism; D001665:Binding Sites; D004926:Escherichia coli / Q000378:metabolism; D010452:Peptide Biosynthesis; D010441:Peptide Chain Elongation, Translational; D011485:Protein Binding; D012343:RNA, Transfer / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism*
D000596:Amino Acids; D012343:RNA, Transfer