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. 1972 Mar;69(3):733-6.
doi: 10.1073/pnas.69.3.733.

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

B Cabrer, D Vázquez, J Modolell

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

B Cabrer et al. Proc Natl Acad Sci U S A. 1972 Mar.

Abstract

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.

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