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| Item Type: | Article |
|---|---|
| Title: | Phosphorylation of elongation factor Tu prevents ternary complex formation |
| Creators Name: | Alexander, C., Bilgin, N., Lindschau, C., Mesters, J.R., Kraal, B., Hilgenfeld, R., Erdmann, V.A. and Lippmann, C. |
| 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. |
| Keywords: | Anti-Bacterial Agents, Computer Graphics, Escherichia Coli, Molecular Models, Peptide Elongation Factor Tu, Phosphorylation, Protein Conformation, Post-Protein Processing, Pyridones, Amino Acyl Transfer RNA |
| Source: | Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Volume: | 270 |
| Number: | 24 |
| Page Range: | 14541-14547 |
| Date: | 16 June 1995 |
| Official Publication: | https://doi.org/10.1074/jbc.270.24.14541 |
| PubMed: | View item in PubMed |
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