The Interaction of Elongation Factor G with N-Acetylphenylalanyl Transfer RNA·Ribosme Complexes

摘要: Abstract N-Acetyl-Phe-tRNA, nonenzymically bound to the acceptor site of Escherichia coli ribosomes, readily undergoes translocation in presence elongation factor (EF)-G and GTP. The translocated N-acetyl-Phe-tRNA, ribosomal donor site, prevents further interaction EF-G with ribosome, for it inhibits GTP hydrolysis that takes place ribosomes decreases formation either GDP·EF-G·fusidic acid·ribosome complex or 5′-guanylylmethylenediphosphonate·EF-G·ribosome complex. Deacylation puromycin site-bound N-acetyl-Phe-tRNA reverses these inhibitions, even though tRNAPhe moiety remains ribosme. These results suggest complexed messenger RNA peptidyl-tRNA may be restricted their ability interact part cycle when is deacylated tRNA site. associated peptide bond control ribosome.