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

  • E. Vijgenboom
  • L. Nilsson
  • A. Talens
  • L. Bosch

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).

Keywords

Elongation Factor Guanine Nucleotide Binding Protein Polypeptide Synthesis Selective Inactivation Strain PM816 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • E. Vijgenboom
    • 1
  • L. Nilsson
    • 1
  • A. Talens
    • 1
  • L. Bosch
    • 1
  1. 1.Department of BiochemistryLeiden UniversityLeidenThe Netherlands

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