Abstract
Among the various factors needed for protein biosynthesis on the ribosome, the elongation factor Tu (EF-Tu)3 is the one which in recent years has attracted most attention (for refs see Miller and Weissbach 1977; Bermek 1978; Clark 1980; Parmeggiani and Sander 1980, 1981; Bosch et al. 1983). Because of its remarkable properties and multifunctional activities, EF-Tu can be considered as a model for the investigation of allosteric mechanisms as well as of protein-protein, protein-nucleic acid, and protein nucleotide interactions. The interaction between EF-Tu and aa-tRNA has been object of numerous publications (Gordon 1968; Shorey et al. 1969; Beres and Lucas-Lenard 1973; Ringer and Chladek 1975; Pingoud et al. 1977; Sprinzl et al. 1978; Boutorin et al. 1981; Kao et al. 1983; Wikman et al. 1983). The techniques used were different, but until recently none of them concerned the GTPase activity of the factor. The results of these studies pointed to the importance of the aminoacylation and of the 3’ extremity for the interaction with EF-Tu, while leaving many open questions about the participation and role of the individual nucleotidyl residues and sequences of the 3’ extremity as well as of the other domains of the aa-tRNA molecule. For this reason, 4 years ago we decided to start the investigation of the interaction between EF-Tu and aa-tRNA by utilizing as a probe the GTP hydrolysis which is one of the fundamental activities of the factor.
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References
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© 1984 Springer-Verlag, Berlin Heidelberg
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Parmeggiani, A., Parlato, G., Guesnet, J., Picone, D., Pizzano, R., Fasano, O. (1984). Interaction Between Elongation Factor Tu and Aminoacyl-tRNA. In: Bermek, E. (eds) Mechanisms of Protein Synthesis. Proceedings in Life Sciences. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-69912-2_4
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DOI: https://doi.org/10.1007/978-3-642-69912-2_4
Publisher Name: Springer, Berlin, Heidelberg
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