The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

tuf  -  elongation factor Tu

Escherichia coli O157:H7 str. Sakai

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of tuf

  • Location of the tufB promoter of E. coli: cotranscription of tufB with four transfer RNA genes [1].
  • These mutations are clustered in the three-domain junction interface of the crystal structure of the GTP form of Thermus thermophilus EF-Tu [2].
  • If the mutant gene is the tufA gene, the seisitive cells can be made resistant through inactivation of the tufB gene by insertion of the bacteriophage milliunits genome [3].
  • Radioactive elongation factor Tu coded by either the tufA or the tufB gene of Escherichia coli K-12 was isolated from cells incubated with a mixture of radioactive amino acids after infection with the defective lambda phage particles that carry either of these genes [4].
  • Genetic and molecular analysis of the tRNA-tufB operon of the myxobacterium Stigmatella aurantiaca [5].

High impact information on tuf

  • Part of the additional binding energy of cognate tRNA is used to induce conformational changes in the ribosome that stabilize a transition state for GTP hydrolysis by EF-Tu and subsequently result in accelerated accommodation of tRNA into the peptidyl transferase center [6].
  • However, many fundamental questions remain, such as the mechanism of activation of GTP hydrolysis by EF-Tu, and the relationship between decoding and frameshifting [6].
  • In addition, the ability of wild-type tufB to complement kirromycin resistance was determined with deletion plasmids [1].
  • We have carried out experiments to determine the position of the tufB promoter and thus to infer whether these five genes are in a single transcription unit. tufB cloned on plasmids was fused to Tc (in operon fusion) or to lacZ (in gene fusion) [1].
  • The high molar concentration of EF-Tu relative to EF-G or ribosomes is achieved in part by translating tuf mRNA more efficiently than these other mRNAs [7].

Chemical compound and disease context of tuf


Biological context of tuf

  • Translation of mRNA of the last gene product in the operon (EF-Tu) is also probably not inhibited by S7 [13].
  • The results indicate that the major promoter for tufB lies upstream from the four transfer RNA genes, and that there might be at least one weak internal promotor, possibly adjacent to tufB [1].
  • The interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF-Tu for guanine nucleotides [14].
  • Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins [15].
  • The nucleotide sequence (GpCpGpC) from positions -7 to -4 (designating the initiation site of mRNA as position +1) is responsible for the selective inhibition by ppGpp of tufB transcription [16].

Anatomical context of tuf


Associations of tuf with chemical compounds

  • A specific increase in S7 synthesis caused by stimulation in transcription originating from the arabinose promoter decreased the synthetic rate for EF-G but had no effect on S12 or EF-Tu synthesis [13].
  • Thus, enacyloxin IIa can affect both EF-Tu and the ribosomal A-site directly, inducing an anomalous positioning of aa-tRNA, that inhibits the incorporation of the amino acid into the polypeptide chain [19].
  • However, the EF-Tu-dependent binding of aa-tRNA to the ribosomal A-site is impaired only slightly by the antibiotic and the activity of the peptidyl-transferase center, as determined by puromycin reactivity, is not affected [19].
  • First, a strong correlation is observed between stimulation of the GTPase activity and enhancement of the reactivity of Cys-81 of EF-Tu toward N-ethylmaleimide at various concentrations of aminoacyl-tRNA, deacylated tRNA, and N-acetylaminoacyl-tRNA [20].
  • Such an abolishment was achieved by treating EF-Tu extensively with the thiol reagent L-1-tosylamido-2-phenylethyl chloromethyl ketone [20].

Physical interactions of tuf

  • In accordance, the EF-Tu epitopes interacting with EF-Ts are lacking in SelB [21].

Regulatory relationships of tuf

  • The effects of these mutations on the ability of EF-Ts to stimulate GDP exchange with EF-Tu.GDP and on its ability to stimulate the activity of EF-Tu in polymerization were tested [22].

Other interactions of tuf


Analytical, diagnostic and therapeutic context of tuf


  1. Location of the tufB promoter of E. coli: cotranscription of tufB with four transfer RNA genes. Lee, J.S., An, G., Friesen, J.D., Fill, N.P. Cell (1981) [Pubmed]
  2. Pulvomycin-resistant mutants of E.coli elongation factor Tu. Zeef, L.A., Bosch, L., Anborgh, P.H., Cetin, R., Parmeggiani, A., Hilgenfeld, R. EMBO J. (1994) [Pubmed]
  3. Mutants of Escherichia coli altered in both genes coding for the elongation factor Tu. Van de Klundert, J.A., Van der Meide, P.H., Van de Putte, P., Bosch, L. Proc. Natl. Acad. Sci. U.S.A. (1978) [Pubmed]
  4. The elongation factor Tu coded by the tufA gene of Escherichia coli K-12 is almost identical to that coded by the tufB gene. Furano, A.V. J. Biol. Chem. (1977) [Pubmed]
  5. Genetic and molecular analysis of the tRNA-tufB operon of the myxobacterium Stigmatella aurantiaca. Bremaud, L., Fremaux, C., Laalami, S., Cenatiempo, Y. Nucleic Acids Res. (1995) [Pubmed]
  6. Structural insights into translational fidelity. Ogle, J.M., Ramakrishnan, V. Annu. Rev. Biochem. (2005) [Pubmed]
  7. Regulation of the synthesis of E. coli elongation factor Tu. Young, F.S., Furano, A.V. Cell (1981) [Pubmed]
  8. Ligand interactions with eukaryotic translation initiation factor 2: role of the gamma-subunit. Erickson, F.L., Hannig, E.M. EMBO J. (1996) [Pubmed]
  9. Euglena gracilis chloroplast elongation factor Tu. Purification and initial characterization. Sreedharan, S.P., Beck, C.M., Spremulli, L.L. J. Biol. Chem. (1985) [Pubmed]
  10. Elongation factor 1 alpha from Saccharomyces cerevisiae. Rapid large-scale purification and molecular characterization. Thiele, D., Cottrelle, P., Iborra, F., Buhler, J.M., Sentenac, A., Fromageot, P. J. Biol. Chem. (1985) [Pubmed]
  11. Nucleotide sequence of a Euglena gracilis chloroplast genome region coding for the elongation factor Tu; evidence for a spliced mRNA. Montandon, P.E., Stutz, E. Nucleic Acids Res. (1983) [Pubmed]
  12. Export of the siderophore enterobactin in Escherichia coli: involvement of a 43 kDa membrane exporter. Furrer, J.L., Sanders, D.N., Hook-Barnard, I.G., McIntosh, M.A. Mol. Microbiol. (2002) [Pubmed]
  13. Identification of ribosomal protein S7 as a repressor of translation within the str operon of E. coli. Dean, D., Yates, J.L., Nomura, M. Cell (1981) [Pubmed]
  14. The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution. Kawashima, T., Berthet-Colominas, C., Wulff, M., Cusack, S., Leberman, R. Nature (1996) [Pubmed]
  15. Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins. Jurnak, F. Science (1985) [Pubmed]
  16. Regulation of the expression of the tufB operon: DNA sequences directly involved in the stringent control. Mizushima-Sugano, J., Kaziro, Y. EMBO J. (1985) [Pubmed]
  17. In vitro methylation of the elongation factor EF-Tu from Escherichia coli. Toledo, H., Jerez, C.A. FEBS Lett. (1985) [Pubmed]
  18. 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]
  19. Enacyloxin IIa, an inhibitor of protein biosynthesis that acts on elongation factor Tu and the ribosome. Cetin, R., Krab, I.M., Anborgh, P.H., Cool, R.H., Watanabe, T., Sugiyama, T., Izaki, K., Parmeggiani, A. EMBO J. (1996) [Pubmed]
  20. GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site. Van Noort, J.M., Kraal, B., Bosch, L. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  21. Structural model for the selenocysteine-specific elongation factor SelB. Hilgenfeld, R., Böck, A., Wilting, R. Biochimie (1996) [Pubmed]
  22. Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor Tu. Zhang, Y., Yu, N.J., Spremulli, L.L. J. Biol. Chem. (1998) [Pubmed]
  23. Secondary structure as primary determinant of the efficiency of ribosomal binding sites in Escherichia coli. Looman, A.C., Bodlaender, J., de Gruyter, M., Vogelaar, A., van Knippenberg, P.H. Nucleic Acids Res. (1986) [Pubmed]
  24. Binding interaction between Tet(M) and the ribosome: requirements for binding. Dantley, K.A., Dannelly, H.K., Burdett, V. J. Bacteriol. (1998) [Pubmed]
  25. Site-directed mutagenesis of elongation factor Tu. The functional and structural role of residue Cys81. Anborgh, P.H., Parmeggiani, A., Jonák, J. Eur. J. Biochem. (1992) [Pubmed]
  26. L-glutamate enhances the expression of Thermus maltogenic amylase in Escherichia coli. Jung, H.M., Park, K.H., Kim, S.Y., Lee, J.K. Biotechnol. Prog. (2004) [Pubmed]
  27. Characterization of a limited trypsin digestion form of eukaryotic elongation factor 1 alpha. Kinzy, T.G., Merrick, W.C. J. Biol. Chem. (1991) [Pubmed]
  28. Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA. Abrahams, J.P., Kraal, B., Clark, B.F., Bosch, L. Nucleic Acids Res. (1991) [Pubmed]
  29. The elongation factor EF-Tu from E. coli binds to the upstream activator region of the tRNA-tufB operon. Vijgenboom, E., Nilsson, L., Bosch, L. Nucleic Acids Res. (1988) [Pubmed]
WikiGenes - Universities