Phosphorylation of elongation factor Tu prevents ternary complex formation

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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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