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

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Abstract
The 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.