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Gene Review:

tuf - elongation factor Tu

Escherichia coli CFT073

Mayer, F., Dahl, L.D. et al., Rinas, U. et al., Tapio, S. et al.

Mayer,

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Disease relevance of tuf

A feature that is common to both bacteria and to Thermoanaerobacterium sp. appears to be that the lining and the fibrils crossing the cytoplasm contain a high number of copies of the bacterial elongation factor Tu (EF-Tu) [1].
Base 2661 in Escherichia coli 23S rRNA influences the binding of elongation factor Tu during protein synthesis in vivo [2].

High impact information on tuf

The mutations had no effect on EF-Tu-dependent delivery of aminoacyl-tRNA to the ribosome [3].
An important feature of the nucleotide exchange is the structural rearrangement of EF-Tu in the EF-Tu.EF-Ts complex caused by insertion of Phe-81 of EF-Ts between His-84 and His-118 of EF-Tu [3].
The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange [3].
These inclusion bodies additionally contain significant amounts of the heat-shock chaperone DnaK, and putative DnaK substrates such as the elongation factor Tu (ET-Tu) and the metabolic enzymes dihydrolipoamide dehydrogenase (LpdA), tryptophanase (TnaA), and d-tagatose-1,6-bisphosphate aldolase (GatY) [4].
Current research and developmental efforts are aimed at the design of a new class of antibacterial drugs, acting by destabilization of the EF-Tu-containing bacterial cytoskeleton, and of an innovative mode of inducible lysis of recombinant bacteria by controlled destabilization of the EF-Tu-containing cytoskeleton [1].

References

Cytoskeletal Elements in Bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as Revealed by Electron Microscopy. Mayer, F. J. Mol. Microbiol. Biotechnol. (2006) [Pubmed]
Base 2661 in Escherichia coli 23S rRNA influences the binding of elongation factor Tu during protein synthesis in vivo. Tapio, S., Isaksson, L.A. Eur. J. Biochem. (1991) [Pubmed]
The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange. Dahl, L.D., Wieden, H.J., Rodnina, M.V., Knudsen, C.R. J. Biol. Chem. (2006) [Pubmed]
Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. Rinas, U., Hoffmann, F., Betiku, E., Estap??, D., Marten, S. J. Biotechnol. (2007) [Pubmed]

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