A study of the interaction of Escherichia coli elongation factor-Tu with aminoacyl-tRNAs by partial digestion with cobra venom ribonuclease |
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| Authors: | Alexander S Boutorin Brian FC Clark Jean Pierre Ebel Torben A Kruse Hans Uffe Petersen Pierre Remy Stanislav Vassilenko |
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| Institution: | 1. Institute de Biologie Moléculaire et Cellulaire du CNRS Laboratoire de Biochimie 15, rue René Descartes, 67084 Strasbourg Cedex, France;2. Division of Biostructural Chemistry, Chemistry Department Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark;3. Institute of Organic Chemistry Siberian Branch of the U.S.S.R., Academy of Sciences Novosibirsk, 90, U.S.S.R. |
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| Abstract: | The hydrolysis of several aminoacylated transfer RNAs, by double-strand-specific ribonuclease from Naja oxiana was studied. The sensitivity to this enzyme of Phe-tRNAPhe, Glu-tRNAGlu and Met-tRNAmMet from Escherichia coli and Phe-tRNAPhe from yeast was examined, both in the free state and complexed to E. coli elongation factor Tu. The hydrolysis patterns in the isolated state were similar for all aminoacylated tRNAs except Glu-tRNA2Glu, which exhibited striking differences probably arising from the existence of several subpopulations of tRNA2Glu. When engaged in a ternary complex with EF-Tu and GTP, the aminoacyl-tRNAs were efficiently protected in the amino acid acceptor and TΨC helices, showing that the interaction with EF-Tu primarily takes place at the -C-C-A end and at the amino acid acceptor and TΨC helices. In all cases an increased reactivity of the anticodon stem was observed in the complexed tRNA, possibly resulting from a conformational change in this region of the tRNAs. |
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| Keywords: | Author to whom correspondence should be addressed |
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