Gene Review:
tuf - elongation factor Tu
Escherichia coli O157:H7 str. EDL933
- Mutagenesis of Arg335 in bovine mitochondrial elongation factor Tu and the corresponding residue in the Escherichia coli factor affects interactions with mitochondrial aminoacyl-tRNAs. Hunter, S.E., Spremulli, L.L. RNA biology (2004)
- Cytoskeletal Elements in Bacteria Mycoplasma pneumoniae, Thermoanaerobacterium sp., and Escherichia coli as Revealed by Electron Microscopy. Mayer, F. J. Mol. Microbiol. Biotechnol. (2006)
- Direct demonstration of duplicate tuf genes in enteric bacteria. Furano, A.V. Proc. Natl. Acad. Sci. U.S.A. (1978)
- A novel translation initiation region from Mycoplasma genitalium that functions in Escherichia coli. Loechel, S., Inamine, J.M., Hu, P.C. Nucleic Acids Res. (1991)
- Structure and expression of elongation factor Tu from Bacillus stearothermophilus. Krásný, L., Mesters, J.R., Tieleman, L.N., Kraal, B., Fucík, V., Hilgenfeld, R., Jonák, J. J. Mol. Biol. (1998)
- Toward a model for the interaction between elongation factor Tu and the ribosome. Weijland, A., Parmeggiani, A. Science (1993)
- Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. Valle, M., Sengupta, J., Swami, N.K., Grassucci, R.A., Burkhardt, N., Nierhaus, K.H., Agrawal, R.K., Frank, J. EMBO J. (2002)
- Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. Pape, T., Wintermeyer, W., Rodnina, M.V. EMBO J. (1998)
- The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome. Vorstenbosch, E., Pape, T., Rodnina, M.V., Kraal, B., Wintermeyer, W. EMBO J. (1996)
- Three tuf-like genes in the kirromycin producer Streptomyces ramocissimus. Vijgenboom, E., Woudt, L.P., Heinstra, P.W., Rietveld, K., van Haarlem, J., van Wezel, G.P., Shochat, S., Bosch, L. Microbiology (Reading, Engl.) (1994)
- Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography. la Cour, T.F., Nyborg, J., Thirup, S., Clark, B.F. EMBO J. (1985)
- The tRNA specificity of Thermus thermophilus EF-Tu. Asahara, H., Uhlenbeck, O.C. Proc. Natl. Acad. Sci. U.S.A. (2002)
- Single turnover kinetic studies of guanosine triphosphate hydrolysis and peptide formation in the elongation factor Tu-dependent binding of aminoacyl-tRNA to Escherichia coli ribosomes. Thompson, R.C., Dix, D.B., Eccleston, J.F. J. Biol. Chem. (1980)
- EPR studies of the Mn(II) complex with elongation factor Tu and GDP Identification of oxygen ligands to Mn(II) by observation of 17O superhyperfine coupling. Eccleston, J.F., Webb, M.R., Ash, D.E., Reed, G.H. J. Biol. Chem. (1981)
- Homologous recombination between the tuf genes of Salmonella typhimurium. Abdulkarim, F., Hughes, D. J. Mol. Biol. (1996)
- Monoclonal antibodies specific for elongation factor Tu and complete nucleotide sequence of the tuf gene in Mycobacterium tuberculosis. Carlin, N.I., Löfdahl, S., Magnusson, M. Infect. Immun. (1992)
- 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)
- Precursors of three exported proteins in Escherichia coli. Randall, L.L., Hardy, S.J., Josefsson, L.G. Proc. Natl. Acad. Sci. U.S.A. (1978)
- Natural kirromycin resistance of elongation factor Tu from the kirrothricin producer Streptomyces cinnamoneus. Cappellano, C., Monti, F., Sosio, M., Donadio, S., Sarubbi, E. Microbiology (Reading, Engl.) (1997)
- 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)
- Mutant ribosomes can generate dominant kirromycin resistance. Tubulekas, I., Buckingham, R.H., Hughes, D. J. Bacteriol. (1991)
- Analysis, characterization, and loci of the tuf genes in lactobacillus and bifidobacterium species and their direct application for species identification. Ventura, M., Canchaya, C., Meylan, V., Klaenhammer, T.R., Zink, R. Appl. Environ. Microbiol. (2003)
- Functional effects of deleting the coiled-coil motif in Escherichia coli elongation factor Ts. Karring, H., Björnsson, A., Thirup, S., Clark, B.F., Knudsen, C.R. Eur. J. Biochem. (2003)
- Properties of a genetically engineered G domain of elongation factor Tu. Parmeggiani, A., Swart, G.W., Mortensen, K.K., Jensen, M., Clark, B.F., Dente, L., Cortese, R. Proc. Natl. Acad. Sci. U.S.A. (1987)
- Crystal structure of Escherichia coli phosphoenolpyruvate carboxykinase: a new structural family with the P-loop nucleoside triphosphate hydrolase fold. Matte, A., Goldie, H., Sweet, R.M., Delbaere, L.T. J. Mol. Biol. (1996)
- Elongation factor Tu and DnaK are transferred from the cytoplasm to the periplasm of Escherichia coli during osmotic downshock presumably via the mechanosensitive channel mscL. Berrier, C., Garrigues, A., Richarme, G., Ghazi, A. J. Bacteriol. (2000)
- A mutant of Escherichia coli with an altered elongation factor Tu. Pedersen, S., Blumenthal, R.M., Reeh, S., Russell, L.B., Lemaux, P., Laursen, R.A., Nagarkatti, S., Friesen, J.D. Proc. Natl. Acad. Sci. U.S.A. (1976)
- The amino acid sequence of elongation factor Tu of Escherichia coli. The large cyanogen bromide peptides. L'Italien, J.J., Laursen, R.A. J. Biol. Chem. (1981)
- The elongation factor Tu from Escherichia coli, aminoacyl-tRNA, and guanosine tetraphosphate form a ternary complex which is bound by programmed ribosomes. Pingoud, A., Gast, F.U., Block, W., Peters, F. J. Biol. Chem. (1983)
- Precursor for elongation factor Tu from Escherichia coli. Lifson, E.R., Lindahl, L., Zengel, J.M. J. Bacteriol. (1986)