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Gene Review:

tuf - elongation factor Tu

Escherichia coli O157:H7 str. Sakai

Rinas, U. et al., Marchant, A. et al., Tapio, S. et al.

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Disease relevance of tuf

Base 2661 in Escherichia coli 23S rRNA influences the binding of elongation factor Tu during protein synthesis in vivo [1].

High impact information on tuf

Two of the bases mutated (at positions A2660 and G2661) have been implicated in the binding of both elongation factor Tu and elongation factor G to the ribosome [Moazed, D., Robertson, J. M. & Noller, H. F. (1988) Nature 334, 362-364] [2].
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) [3].

References

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]
Mutational studies on the alpha-sarcin loop of Escherichia coli 23S ribosomal RNA. Marchant, A., Hartley, M.R. Eur. J. Biochem. (1994) [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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