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  • Title: Interaction of methionine-specific tRNAs from Escherichia coli with immobilized elongation factor Tu.
    Author: Fischer W, Doi T, Ikehara M, Ohtsuka E, Sprinzl M.
    Journal: FEBS Lett; 1985 Nov 11; 192(1):151-4. PubMed ID: 3902504.
    Abstract:
    The interaction of three different Met-tRNAsMet from E. coli with bacterial elongation factor (EF) Tu X 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 X 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 X 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 X EF-Tu X GTP ternary complex formation.
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