A New Concept of the Function of Elongation Factor 1 in Peptide Chain Elongation

Publisher Website
Google Scholar
Abstract
An entirely new model for the mechanism of elongation factor 1 (EF‐1) function is presented. Experiments, in which mixtures of [3H]EF‐1, ribosomes from Krebs II ascites cells and various additional co‐factors were analyzed by chromatography on Sepharose 6B, show that EF‐1 binds to the ribosome early in the translation process and remains bound on the ribosome during translation. Optimal EF‐1 binding occurs on polynucleotide‐programmed ribosomes carrying a tRNA in their P‐site. On the other hand it was clearly shown that EF‐2 attached at each translocation event and was then released before a new Phe‐tRNA could be bound.