It is well established that peptide bond formation during protein synthesis in E. coli is catalyzed by the 50 S ribosomal subunit and it has been proposed that the catalytic agent is an enzyme, peptidyl transferase, integrated into the subunit structure (Monro, Staehelin, Celma, and Vazquez, this volume). 70 S ribosomes from other bacterial species have been shown to be very similar to those of E. coli in this respect (Vazquez, Celma, Fernandez-Muñoz, and Monro, unpubl.), but corresponding studies have not hitherto been reported with 80 S ribosomes. Indeed, it has been widely believed since the work of Arlinghaus, Schaeffer,and Schweet (1964), that a supernatant protein, TF-1, is responsible for catalysis of peptide bond formation in mammalian cytoplasm. However, it has been suggested that the reaction might be ribosome-catalyzed in view of the reactivity with puromycin of nascent protein on washed 80 S ribosomes from rat liver (Skogerson and Moldave,...
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Vázquez et al. (1969) studied this question.