Abstract
A highly representative member of the group of guanine nucleotide binding proteins is the polypeptide chain elongation factor Tu of E. coli (EF-Tu). This translational factor is a multifunctional protein able to bind, beside GDP and GTP, a relatively large number of ligands, such as tRNA, ribosomes, the elongation factor EF-Ts and antibiotics like kirromycin and pulvomycin. EF-Tu is also involved in the replication of RNA phages as one of the host donated subunits of the viral RNA replicase (Miller et al., 1977; Bosch et al., 1983; Bosch et al., 1986). EF-Tu therefore is an attractive object for studies of the relationship between structure and function. Considerable progress has been made with the elucidation of the three-dimensional structure of EF-Tu as is reported elsewhere in this volume (Jurnak et al., 1989; Nyborg et al., 1989). Genetic studies revealed that EF-Tu is encoded by two genes: tufA and tufB, located some 660 kbp apart on the E. coli chromosome (Jaskunas et al., 1975). The two genes have been cloned and sequenced (An and Friesen, 1980; Yokota et al., 1980; Hudson et al., 1981) so that a firm experimental basis has been laid for structure/function studies. They are part of two operons quite different in character (compare Fig. 1).
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Vijgenboom, E., Nilsson, L., Talens, A., Bosch, L. (1989). The Elongation Factor EF-Tu FROM E. Coli Activates The tRNA-Tufb Operon in Trans by Binding To A Cis-Acting Region Upstream of The Promoter. In: Bosch, L., Kraal, B., Parmeggiani, A. (eds) The Guanine — Nucleotide Binding Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2037-2_6
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DOI: https://doi.org/10.1007/978-1-4757-2037-2_6
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