Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu

AbstractThe interaction of three different Met-tRNAsMet from E. coli with bacterial elongation factor (EF) Tu · GTP was investigated by affinity chromatography. Met-tRNAfMet which lacks the base pair at the end of the acceptor stem binds only weakly to EF-Tu·GTP, while Met-tRNAmMet has a high affinity for the elongation factor. A modified Met-tRNAfMet which has a C1-G72 base pair binds much more strongly to immobilized EF-Tu·GTP than the native aminoacyl(aa)-tRNA with non-base-paired C1A72 at this position, demonstrating that the base pair including the first nucleotide in the tRNA is one of the essential structural requirements for the aa-tRNA·EF-Tu·GTP ternary complex formation