PMID:7782317
| Citation |
Alexander, C, Bilgin, N, Lindschau, C, Mesters, JR, Kraal, B, Hilgenfeld, R, Erdmann, VA and Lippmann, C (1995) Phosphorylation of elongation factor Tu prevents ternary complex formation. J. Biol. Chem. 270:14541-7 |
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| Abstract |
The elongation factor Tu (EF-Tu) is a member of the GTP/GDP-binding proteins and interacts with various partners during the elongation cycle of protein biosynthesis thereby mediating the correct binding of amino-acylated transfer RNA (aa-tRNA) to the acceptor site (A-site) of the ribosome. After GTP hydrolysis EF-Tu is released in its GDP-bound state. In vivo, EF-Tu is post-translationally modified by phosphorylation. Here we report that the phosphorylation of EF-Tu by a ribosome associated kinase activity is drastically enhanced by EF-Ts. The antibiotic kirromycin, known to block EF-Tu function, inhibits the modification. This effect is specific, since kirromycin-resistant mutants do become phosphorylated in the presence of the antibiotic. On the other hand, phosphorylated wild-type EF-Tu does not bind kirromycin. Most interestingly, the phosphorylation of EF-Tu abolishes its ability to bind aa-tRNA. In the GTP conformation the site of modification is located at the interface between domains 1 and 3 and is involved in a strong interdomain hydrogen bond. Introduction of a charged phosphate group at this position will change the interaction between the domains, leading to an opening of the molecule reminiscent of the GDP conformation. A model for the function of EF-Tu phosphorylation in protein biosynthesis is presented. |
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| Keywords |
Anti-Bacterial Agents/metabolism; Computer Graphics; Escherichia coli/metabolism; Models, Molecular; Peptide Elongation Factor Tu/chemistry; Peptide Elongation Factor Tu/metabolism; Peptide Elongation Factors/metabolism; Phosphorylation; Protein Conformation; Protein Processing, Post-Translational; Pyridones/metabolism; RNA, Transfer, Amino Acyl/metabolism |
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