A new concept of the function of elongation factor 1 in peptid chain elongation.
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 Drebs 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.
D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000031:analogs & derivatives / Q000378:metabolism; D051379:Mice; D010441:Peptide Chain Elongation, Translational; D010445:Peptide Elongation Factors; D010649:Phenylalanine; D012343:RNA, Transfer / Q000378:metabolism; D012270:Ribosomes / Q000378:metabolism
D010445:Peptide Elongation Factors; D010649:Phenylalanine; D006160:Guanosine Triphosphate; D012343:RNA, Transfer