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. 1982;1(9):1095–1100. doi: 10.1002/j.1460-2075.1982.tb01302.x

The site of interaction of aminoacyl-tRNA with elongation factor Tu.

F P Wikman, G E Siboska, H U Petersen, B F Clark
PMCID: PMC553168  PMID: 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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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