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  • Title: The site of interaction of aminoacyl-tRNA with elongation factor Tu.
    Author: Wikman FP, Siboska GE, Petersen HU, Clark BF.
    Journal: EMBO J; 1982; 1(9):1095-100. PubMed ID: 6765239.
    Abstract:
    We have used RNases T1, T2 and A to digest two aminoacyl-tRNAs, Escherichia coli Phe-tRNAPhe and E. coli Met- tRNAMetm both in the naked forms and in ternary complexes with E. coli elongation factor Tu (EF-Tu) and GTP. An analysis of the 'footprinting' results has led to an interpretation that has localized the part of the three-dimensional structure of aminoacyl-tRNA covered by the protein in the ternary complex. In terms of the three-dimensional structure of tRNA established for yeast tRNAPhe, EF-Tu covers the aa-end, aa-stem, T-stem, and extra loop on the side of the L-shaped tRNA that exposes the extra loop.
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