Gene Symbol: tufB
Description: translation elongation factor EF-Tu 2
Alias: ECK3971, JW3943, kirT, pulT
Species: Escherichia coli str. K-12 substr. MG1655
Products:     tufB

Top Publications

  1. Cochella L, Green R. An active role for tRNA in decoding beyond codon:anticodon pairing. Science. 2005;308:1178-80 pubmed
    ..These data provide evidence for a direct role for tRNA in signaling its own acceptance during decoding and support its fundamental role during the evolution of protein synthesis. ..
  2. Valle M, Sengupta J, Swami N, Grassucci R, Burkhardt N, Nierhaus K, et al. Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process. EMBO J. 2002;21:3557-67 pubmed publisher
  3. Valle M, Zavialov A, Li W, Stagg S, Sengupta J, Nielsen R, et al. Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy. Nat Struct Biol. 2003;10:899-906 pubmed
    ..From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome. ..
  4. van Noort J, Kraal B, Bosch L, la Cour T, Nyborg J, Clark B. Cross-linking of tRNA at two different sites of the elongation factor Tu. Proc Natl Acad Sci U S A. 1984;81:3969-72 pubmed
    ..In both elongation factor Tu complexes, kirromycin itself was found cross-linked to lysine-357. The tRNA cross-linking sites are in agreement with the idea of two different binding sites of tRNA on elongation factor Tu. ..
  5. Miller D, Cashel M, Weissbach H. The interaction of guanosine 5'-diphosphate, 2' (3')-diphosphate with the bacterial elongation factor Tu. Arch Biochem Biophys. 1973;154:675-82 pubmed
  6. Hachmann J, Miller D, Weissbach H. Purification of factor Ts: studies on the formation and stability of nucleotide complexes containing transfer factor Tu. Arch Biochem Biophys. 1971;147:457-66 pubmed
  7. Miyajima A, Yokota T, Takebe Y, Nakamura M, Kaziro Y. A deletion mutant lacking three out of four transfer RNA genes upstream of the coding region of tufB. J Biochem. 1983;93:1101-8 pubmed
    Of the two plasmids pTUB1 and pTUB2 constructed by cloning of the 8.9 kb EcoRI fragment carrying tufB (Miyajima, A., Shibuya, M., & Kaziro, Y. (1979) FEBS Lett. 102, 207-210), pTUB2 possesses a deletion of about 0.3 kb...
  8. Kristensen O, Reshetnikova L, Nissen P, Siboska G, Thirup S, Nyborg J. Isolation, crystallization and X-ray analysis of the quaternary complex of Phe-tRNA(Phe), EF-Tu, a GTP analog and kirromycin. FEBS Lett. 1996;399:59-62 pubmed
    ..Crystals of the mesophilic complex belong to the cubic space P432, with cell axis of 196.26 A. In both cases, the crystals contain one complex per asymmetric unit. ..
  9. Furano A. Direct demonstration of duplicate tuf genes in enteric bacteria. Proc Natl Acad Sci U S A. 1978;75:3104-8 pubmed
    ..Both the K-12 and the B strains of Escherichia coli contain two tuf genes, but no more than two. Salmonella typhimurium also contains duplicate tuf genes. ..

More Information

Publications101 found, 100 shown here

  1. Gumusel F, Cool R, Weijland A, Anborgh P, Parmeggiani A. Mutagenesis of the NH2-terminal domain of elongation factor Tu. Biochim Biophys Acta. 1990;1050:215-21 pubmed
    ..This demonstrates the crucial role of the base specificity for the active conformation of EF-Tu. The obtained results are discussed in the light of the three-dimensional structure of EF-Tu. ..
  2. Miller D, Weissbach H. Studies on the purification and properties of factor Tu from E. coli. Arch Biochem Biophys. 1970;141:26-37 pubmed
  3. Yokota T, Sugisaki H, Takanami M, Kaziro Y. The nucleotide sequence of the cloned tufA gene of Escherichia coli. Gene. 1980;12:25-31 pubmed
    ..Comparison of the tufA nucleotide sequence with the tufB sequence (An and Friesen, 1980) and the known amino acid sequence of EF-Tu (Arai et al...
  4. Wiborg O, Andersen C, Knudsen C, Clark B, Nyborg J. Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA. J Biol Chem. 1996;271:20406-11 pubmed
    ..Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl-tRNA. ..
  5. Caldas T, El Yaagoubi A, Richarme G. Chaperone properties of bacterial elongation factor EF-Tu. J Biol Chem. 1998;273:11478-82 pubmed
    ..These results suggest that EF-Tu, in addition to its function in translation elongation, might be implicated in protein folding and protection from stress. ..
  6. Wahba A, Miller M, Niveleau A, Landers T, Carmichael G, Weber K, et al. Subunit I of G beta replicase and 30 S ribosomal protein S1 of Escherichia coli. Evidence for the identity of the two proteins. J Biol Chem. 1974;249:3314-6 pubmed
  7. Dombou M, Bhide S, Mizushima S. Appearance of elongation factor Tu in the outer membrane of sucrose-dependent spectinomycin-resistant mutants of Escherichia coli. Eur J Biochem. 1981;113:397-403 pubmed
    ..It is suggested that the ribosomal alteration resulted in dislocation of the cytosol protein into the outer membrane. ..
  8. Miyajima A, Kaziro Y. The expression of the cloned tufB gene in vivo. FEBS Lett. 1980;119:215-8 pubmed
  9. Sanderová H, Hůlková M, Malon P, Kepková M, Jonak J. Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms. Protein Sci. 2004;13:89-99 pubmed
    ..It was lower in the GTP conformation, and the mechanism involved the destabilization of the alpha-helical regions of the G-domain by Ecdomain 2. ..
  10. Sanderson L, Uhlenbeck O. The 51-63 base pair of tRNA confers specificity for binding by EF-Tu. RNA. 2007;13:835-40 pubmed
    ..While this contact is an important specificity determinant, it is clear that others remain to be identified. ..
  11. Hori K, Harada K, Kuwano M. Function of bacteriophage Qbeta replicase containing an altered subunit IV. J Mol Biol. 1974;86:699-708 pubmed
  12. Young F, Furano A. Regulation of the synthesis of E. coli elongation factor Tu. Cell. 1981;24:695-706 pubmed
    Rapidly growing E. coli with two active genes (tufA, tufB) for elongation factor (EF) Tu contains three times as much EF-Tu (tuf) mRNA as EF-G (fus) mRNA on a molar basis, but about seven times as much EF-Tu as EF-G or ribosomes...
  13. Laursen R, L Italien J, Nagarkatti S, Miller D. The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence. J Biol Chem. 1981;256:8102-9 pubmed
    ..Structural features of the aminoacyl-tRNA binding site are discussed in the light of sequence and other chemical and biochemical data...
  14. Kamen R. Characterization of the subunits of Q-beta replicase. Nature. 1970;228:527-33 pubmed
  15. Talens A, Boon K, Kraal B, Bosch L. Translational activities of EF-Tu [G222D] which cannot be reconciled with the classical scheme of the polypeptide chain elongation cycle. Biochem Biophys Res Commun. 1996;225:961-7 pubmed
    ..Vijgenboom, E., & Zeef, L.A.H., 1996, Biochemistry 36). ..
  16. Polekhina G, Thirup S, Kjeldgaard M, Nissen P, Lippmann C, Nyborg J. Helix unwinding in the effector region of elongation factor EF-Tu-GDP. Structure. 1996;4:1141-51 pubmed
    ..This change is presumably involved in triggering the release of tRNA, and EF-Tu, from the ribosome...
  17. Clark B, Thirup S, Kjeldgaard M, Nyborg J. Structural information for explaining the molecular mechanism of protein biosynthesis. FEBS Lett. 1999;452:41-6 pubmed
    ..Other translation factors such as the initiation factor-2 and the release factor 1 or 2 are also thought to mimic tRNA. These observations raise questions concerning the possible evolution of G-proteins involved in protein biosynthesis. ..
  18. van de Klundert J, van der Meide P, van de Putte P, Bosch L. Mutants of Escherichia coli altered in both genes coding for the elongation factor Tu. Proc Natl Acad Sci U S A. 1978;75:4470-3 pubmed
    ..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...
  19. Jacobson G, Rosenbusch J. A functionally active tryptic fragment of Escherichia coli elongation factor Tu. Biochemistry. 1976;15:5105-110 pubmed
  20. Kjeldgaard M, Nyborg J. Refined structure of elongation factor EF-Tu from Escherichia coli. J Mol Biol. 1992;223:721-42 pubmed
    ..Elongation factor Tu interacts with proteins, nucleic acids and nucleotides, making this molecule well suited as a model system for the study of these interactions. ..
  21. Blumenthal T, Landers T, Weber K. Bacteriophage Q replicase contains the protein biosynthesis elongation factors EF Tu and EF Ts. Proc Natl Acad Sci U S A. 1972;69:1313-7 pubmed
    ..In addition, Qbeta replicase activity can be reconstituted from subunits I and II with EF Tu and EF Ts. ..
  22. Ganoza M, Aoki H, Burkhardt N, Murphy B. The ribosome as affinity matrix': efficient purification scheme for translation factors. Biochimie. 1996;78:51-61 pubmed
    ..The procedure markedly simplifies the isolation, in homogeneous form, of all the non-ribosomal proteins required to reconstruct translation. ..
  23. Manchester K. Determination of the kinetics of guanine nucleotide exchange on EF-Tu and EF-Ts: continuing uncertainties. Biochem Biophys Res Commun. 2004;314:1-5 pubmed
    ..Metabolic control analysis has been applied to determine the degree of flux control of the different steps in the pathway. ..
  24. Sanderová H, Jonak J. Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activity. Biochim Biophys Acta. 2005;1752:11-7 pubmed
    ..This can be explained by a stabilization effect of domains 2+3 on alpha-helical regions of the G-domain as revealed by CD spectroscopy. ..
  25. Yu H, Chan Y, Wool I. The identification of the determinants of the cyclic, sequential binding of elongation factors tu and g to the ribosome. J Mol Biol. 2009;386:802-13 pubmed publisher
  26. Jacobson G, Takacs B, Rosenbusch J. Properties of a major protein released from Escherichia coli by osmotic shock. Biochemistry. 1976;15:2297-303 pubmed
    ..These unusual properties, its presumed location, and the observation that it is present in large amounts (approximately 70 000 molecules per cell) suggest a structural role for this protein. ..
  27. Minkoff L, Damadian R. Biological ion exchanger resins: VIII. A preliminary report on actin-like protein in E. coli and the cytotonus concept. Physiol Chem Phys. 1975;7:385-9 pubmed
  28. Weissbach H, Brot N, Miller D, Rosman M, Ertel R. Interaction of guanosine triphosphate with E. coli soluble transfer factors. Cold Spring Harb Symp Quant Biol. 1969;34:419-31 pubmed
  29. Dulebohn D, Choy J, Sundermeier T, Okan N, Karzai A. Trans-translation: the tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decay. Biochemistry. 2007;46:4681-93 pubmed
    ..This review will focus on recent advances in our understanding of the structural properties, mechanistic details, and physiological significance of this unique RNA and its principal protein partners. ..
  30. L Italien J, Laursen R. Location of the site of methylation in elongation factor Tu. FEBS Lett. 1979;107:359-62 pubmed
  31. Furano A. Content of elongation factor Tu in Escherichia coli. Proc Natl Acad Sci U S A. 1975;72:4780-4 pubmed
    ..22 doublings per hour contained about 14 molecules per ribosome. These levels resemble those reported for tRNA, in contrast with the 1:1 ratio of factor to ribosomes reported for elongation factors Ts and G. ..
  32. Nissen P, Thirup S, Kjeldgaard M, Nyborg J. The crystal structure of Cys-tRNACys-EF-Tu-GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure. 1999;7:143-56 pubmed
    ..The structure of the 'kissing complex' shows a quasicontinuous helix with a distinct shape determined by the number of base pairs...
  33. Kjeldgaard M, Nyborg J, Clark B. The GTP binding motif: variations on a theme. FASEB J. 1996;10:1347-68 pubmed
    ..Finally, we discuss the important structures of complexes between GTP binding proteins and their substrates that have appeared in the literature recently. ..
  34. Ames G, Niakido K. In vivo methylation of prokaryotic elongation factor Tu. J Biol Chem. 1979;254:9947-50 pubmed
    ..There is no evidence of turnover of the methyl residues. We attempted to separate the methylated from the nonmethylated form of EF-Tu by isoelectric focusing on polyacrylamide gel, but were unable to do so. ..
  35. van der Meide P, Vijgenboom E, Talens A, Bosch L. The role of EF-Tu in the expression of tufA and tufB genes. Eur J Biochem. 1983;130:397-407 pubmed
    We have studied the regulation of the expression of tufA and tufB, the two genes encoding EF-Tu in Escherichia coli...
  36. Boon K, Krab I, Parmeggiani A, Bosch L, Kraal B. Substitution of Arg230 and Arg233 in Escherichia coli elongation factor Tu strongly enhances its pulvomycin resistance. Eur J Biochem. 1995;227:816-22 pubmed
    ..GDP.pulvomycin complex rather than by EF-Tu.GTP.pulvomycin. Moreover, the mutant [R230V, R233F]EF-TuHis shows a stronger protection of the ester bond of aminoacyl-tRNA than wild-type EF-Tu. ..
  37. Mayer F. Cytoskeletons in prokaryotes. Cell Biol Int. 2003;27:429-38 pubmed
  38. Norris V, Den Blaauwen T, Doi R, Harshey R, Janniere L, Jimenez Sanchez A, et al. Toward a hyperstructure taxonomy. Annu Rev Microbiol. 2007;61:309-29 pubmed
    ..Hence a taxonomy by trajectory may be desirable. Finally, we suggest that working toward a taxonomy based on speculative interactions between hyperstructures promises most insight into life at this level. ..
  39. Minkoff L, Abramowitz J, Damadian R. Biological ion exchanger resins; IX. Isolation and partial identification of a potassium sensitive contractile-like protein from E. coli. Physiol Chem Phys. 1976;8:167-73 pubmed
    ..The fraction contained 30% RNA by weight that proved refractory to experimental efforts at removal. ..
  40. Abrahams J, Acampo J, Kraal B, Bosch L. The influence of tRNA located at the P-site on the turnover of EF-Tu.GTP on ribosomes. Biochimie. 1991;73:1089-92 pubmed
    ..GTP than ribosomes with an empty P-site. The data suggest that this is mainly caused by an increased affinity of EF-Tu.GTP for ribosomes with a filled P-site rather than by an enhanced reactivity of the GTPase centre. ..
  41. van Noort J, Kraal B, Bosch L. GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site. Proc Natl Acad Sci U S A. 1986;83:4617-21 pubmed
    ..EF-Tu X GTP thus treated has lost its ability to protect the ester bond of aminoacyl-tRNA. The relevance of these data for the sequence of events during protein synthesis and for control of translational fidelity is discussed. ..
  42. Schilstra M, Cremers A, Bosch L, Mellema J. Three-dimensional image reconstruction of helical aggregates of trypsin modified elongation factor EF-Tu from Escherichia coli: comparison with the reconstructed image of intact EF-Tu. J Ultrastruct Mol Struct Res. 1986;94:260-7 pubmed
    ..4 subunits per turn and a pitch of 64 A. The shape of the monomeric proteolyzed EF-Tu.GDP in this helical arrangement is very similar to that of the intact molecule in cylindrical assemblies studied at this resolution. ..
  43. Mizushima Sugano J, Miyajima A, Kaziro Y. Selective inhibition of transcription of the E. coli tufB operon by guanosine-5'-diphosphate-3'-diphosphate. Mol Gen Genet. 1983;189:185-92 pubmed
    We have studied the effect of guanosine-5'-diphosphate-3'-diphosphate (ppGpp) on the transcription of the E. coli tufB and recA operons in a cell-free system containing of purified RNA polymerase holoenzyme...
  44. Nyborg J, Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Clark B. Structure of the ternary complex of EF-Tu: macromolecular mimicry in translation. Trends Biochem Sci. 1996;21:81-2 pubmed
  45. Mohr D, Wintermeyer W, Rodnina M. GTPase activation of elongation factors Tu and G on the ribosome. Biochemistry. 2002;41:12520-8 pubmed
    ..This effect appears to be augmented by interactions of other structural elements of the large ribosomal subunit with the switch regions of the factors. ..
  46. Hunter S, Spremulli L. Mutagenesis of glutamine 290 in Escherichia coli and mitochondrial elongation factor Tu affects interactions with mitochondrial aminoacyl-tRNAs and GTPase activity. Biochemistry. 2004;43:6917-27 pubmed
    ..Surprisingly, while E. coli EF-Tu Q290L is more active in polymerization with mitochondrial Phe-tRNA(Phe), this variant has low activity in the formation of a stable ternary complex with mitochondrial aa-tRNA. ..
  47. Rodnina M. Visualizing the protein synthesis machinery: new focus on the translational GTPase elongation factor Tu. Proc Natl Acad Sci U S A. 2009;106:969-70 pubmed publisher
  48. Blumenthal T, Carmichael G. RNA replication: function and structure of Qbeta-replicase. Annu Rev Biochem. 1979;48:525-48 pubmed
  49. Kamen R, Kondo M, Römer W, Weissmann C. Reconstitution of Q replicase lacking subunit with protein-synthesis-interference factor i. Eur J Biochem. 1972;31:44-51 pubmed
  50. Swart G, Kraal B, Bosch L, Parmeggiani A. Allosteric changes of the guanine nucleotide site of elongation factor EF-Tu: a comparative study of two kirromycin-resistant EF-Tu species. FEBS Lett. 1982;142:101-6 pubmed
  51. Cremers A, Bosch L, Mellema J. Characterization of regular polymerization products of elongation factor EF-Tu from Escherichia coli by electron microscopy and image processing. J Mol Biol. 1981;153:477-86 pubmed
  52. Hudson L, Rossi J, Landy A. Dual function transcripts specifying tRNA and mRNA. Nature. 1981;294:422-7 pubmed
  53. Weijland A, Parlato G, Parmeggiani A. Elongation factor Tu D138N, a mutant with modified substrate specificity, as a tool to study energy consumption in protein biosynthesis. Biochemistry. 1994;33:10711-7 pubmed
    ..With rate-limiting amounts of XTP the K'm of its XTPase activity corresponded to the K'm for XTP of poly(phenylalanine) synthesis (0.3-0.6 microM).(ABSTRACT TRUNCATED AT 250 WORDS) ..
  54. Kraal B, Zeef L, Mesters J, Boon K, Vorstenbosch E, Bosch L, et al. Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coli. Biochem Cell Biol. 1995;73:1167-77 pubmed
    ..random and site-directed mutagenesis methods have yielded sets of purified mutant EF-Tu resistant to kirromycin (kirT) or pulvomycin (pulT)...
  55. Kraal B, Lippmann C, Kleanthous C. Translational regulation by modifications of the elongation factor Tu. Folia Microbiol (Praha). 1999;44:131-41 pubmed
    ..Although the Lit cleavage-mechanism may eventually lead to programmed cell death, the very efficient prevention of phage multiplication may be caused by a novel mechanism of in cis inhibition of late T4 mRNA translation. ..
  56. Minkoff L, Damadian R. Actin-like properties from Escherichia coli: concept of cytotonus as the missing link between cell metabolism and the biological ion-exchange resin. J Bacteriol. 1976;125:353-65 pubmed
    ..The possible role of contractile proteins in biological ion exchange is discussed. ..
  57. Abrahams J, Kraal B, Clark B, Bosch L. Isolation and stability of ternary complexes of elongation factor Tu, GTP and aminoacyl-tRNA. Nucleic Acids Res. 1991;19:553-7 pubmed
    ..In the latter procedure, the solubility characteristics of the ternary complexes are highly reminiscent to those of free tRNA. Concentrated samples of EF-Tu.GMPPNP.aminoacyl-tRNA complexes show a high stability. ..
  58. Highland J, Ochsner E, Gordon J, Hasenbank R, Stoffler G. Letter: Inhibition of phenylalanyl-tRNA binding and elongation factor Tu-dependent GTP hydrolysis by antibodies specific for several ribosomal proteins. J Mol Biol. 1974;86:175-8 pubmed
  59. van der Meide P, Kastelein R, Vijgenboom E, Bosch L. tuf gene dosage effects on the intracellular concentration of EF-TuB. Eur J Biochem. 1983;130:409-17 pubmed
    In this paper we have studied the effect of raising the intracellular EF-Tu concentration on the expression of tufB. To this aim cells were transformed with multicopy plasmids carrying either tufA or tufB...
  60. Heffron S, Jurnak F. Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu. Biochemistry. 2000;39:37-45 pubmed
    ..The results presented here provide the details necessary to enhance the solubility of GE2270A without disrupting its inhibitory properties. ..
  61. Melchionna S, Briganti G, Londei P, Cammarano P. Water induced effects on the thermal response of a protein. Phys Rev Lett. 2004;92:158101 pubmed
    ..The results support the notion that the dynamics of vicinal water makes a substantial contribution to the activity optimum of proteins. ..
  62. Kita H, Cho J, Matsuura T, Nakaishi T, Taniguchi I, Ichikawa T, et al. Functional Qbeta replicase genetically fusing essential subunits EF-Ts and EF-Tu with beta-subunit. J Biosci Bioeng. 2006;101:421-6 pubmed
    ..The fused protein, a single-chain alpha-less Qbeta replicase, was mostly found in the soluble fraction and could be readily purified. These results pave the way for the large-scale production of the highly purified form of this enzyme. ..
  63. Wang Y, Qin H, Kudaravalli R, Kirillov S, Dempsey G, Pan D, et al. Single-molecule structural dynamics of EF-G--ribosome interaction during translocation. Biochemistry. 2007;46:10767-75 pubmed
    ..6 state results from the conformational lability of unlocked ribosomes formed during translocation. An idling state, possibly pertinent to regulation of protein synthesis, is detected in some ribosomes in the poly(Phe) system. ..
  64. Villa E, Sengupta J, Trabuco L, LeBarron J, Baxter W, Shaikh T, et al. Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis. Proc Natl Acad Sci U S A. 2009;106:1063-8 pubmed publisher
    ..Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism. ..
  65. Abrahams J, van Raaij M, Ott G, Kraal B, Bosch L. Kirromycin drastically reduces the affinity of Escherichia coli elongation factor Tu for aminoacyl-tRNA. Biochemistry. 1991;30:6705-10 pubmed
    ..Modification with N-tosyl-L-phenylalanine chloromethyl ketone (TPCK) decreases the affinity of EF-Tu-kirromycin-GTP for aminoacyl-tRNA, just like it does in the absence of the antibiotic. ..
  66. Hwang Y, Sanchez A, Miller D. Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteins. J Biol Chem. 1989;264:8304-9 pubmed
    ..These results indicate that EF-Ts is essential to the growth of E. coli and suggest a technique for studying EF-Ts mutants as well as for identifying other guanine nucleotide exchange enzymes. ..
  67. Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark B, et al. Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. Science. 1995;270:1464-72 pubmed
    ..The overall shape of the ternary complex is similar to that of the translocation factor, EF-G-GDP, and this suggests a novel mechanism involving "molecular mimicry" in the translational apparatus. ..
  68. Helms M, Marriott G, Sawyer W, Jameson D. Dynamics and morphology of the in vitro polymeric form of elongation factor Tu from Escherichia coli. Biochim Biophys Acta. 1996;1291:122-30 pubmed
    ..A sub-microsecond motion which was slowed in the presence of glycerol may be due to local flexibility of the polymers. The possible relevance of polymeric EF-Tu to its function in vivo is discussed. ..
  69. Diaconu M, Kothe U, Schl nzen F, Fischer N, Harms J, Tonevitsky A, et al. Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell. 2005;121:991-1004 pubmed publisher
    ..Highly mobile L7/12 C-terminal domains promote recruitment of translation factors to the ribosome and stimulate GTP hydrolysis by the ribosome bound factors through stabilization of their active GTPase conformation...
  70. Furano A. The elongation factor Tu coded by the tufA gene of Escherichia coli K-12 is almost identical to that coded by the tufB gene. J Biol Chem. 1977;252:2154-7 pubmed
    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 ..
  71. Pedersen S, Bloch P, Reeh S, Neidhardt F. Patterns of protein synthesis in E. coli: a catalog of the amount of 140 individual proteins at different growth rates. Cell. 1978;14:179-90 pubmed
    ..Proteins with invariant levels in the various media comprise about 4% of the cell's total protein. ..
  72. Hwang Y, McCabe P, Innis M, Miller D. Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor Tu. Arch Biochem Biophys. 1989;274:394-403 pubmed
  73. Vijgenboom E, Vink T, Kraal B, Bosch L. Mutants of the elongation factor EF-Tu, a new class of nonsense suppressors. EMBO J. 1985;4:1049-52 pubmed
    ..The two phenomena differ essentially. Readthrough of UGA in wild-type cells is reduced by inactivation of tufB but is restored to the original level by introducing into the cell plasmid-borne EF-Tu...
  74. Miyajima A, Shibuya M, Kuchino Y, Kaziro Y. Transcription of the E. coli tufB gene: cotranscription with four tRNA genes and inhibition by guanosine-5'-diphosphate-3'-diphosphate. Mol Gen Genet. 1981;183:13-9 pubmed
    The transcription of the tufB gene by purified RNA polymerase holoenzyme was studied using the transducing phage lambda rifd 18 DNA and the hybrid plasmid pTUB1 DNA (Miyajima et al. 1979) as templates...
  75. van der Meide P, Vijgenboom E, Dicke M, Bosch L. Regulation of the expression of tufA and tufB, the two genes coding for the elongation factor EF-Tu in Escherichia coli. FEBS Lett. 1982;139:325-30 pubmed
  76. Weijland A, Sarfati R, Barzu O, Parmeggiani A. Asparagine-135 of elongation factor Tu is a crucial residue for the folding of the guanine nucleotide binding pocket. FEBS Lett. 1993;330:334-8 pubmed
    ..kirromycin can mediate the binding of aa-tRNA to the mRNA-programmed ribosomes independently of the native conformation of this site. ..
  77. Zheng C, Yang L, Hoopmann M, Eng J, Tang X, Weisbrod C, et al. Cross-linking measurements of in vivo protein complex topologies. Mol Cell Proteomics. 2011;10:M110.006841 pubmed publisher
    ..Furthermore, our unbiased data provide novel in vivo topological information that can impact understanding of biological function, even for cases where high resolution structures are not yet available. ..
  78. Wurtz M, Jacobson R, Steven A, Rosenbusch J. Paracrystalline arrays of protein-synthesis elongation factor Tu. Comparison with polymerized actin. Eur J Biochem. 1978;88:593-7 pubmed
    ..The differences between the surface lattices, in conjunction with the negative results of sensitive immunochemical tests for possible cross-reactivities between the two proteins, suggest that any such relationship is very remote. ..
  79. Furano A. Dissociation of aminoacyl tRNA from the complex of EF-Tu--GTP--aminoacyl tRNA by extracts of Escherichia coli. Biochem Biophys Res Commun. 1976;76:309-16 pubmed
  80. Anborgh P, Cool R, Gumusel F, Harmark K, Jacquet E, Weijland A, et al. Structure-function relationships of elongation factor Tu as studied by mutagenesis. Biochimie. 1991;73:1051-9 pubmed
    ..Concerning the effect of ligands, EF-TuVG20 supports a lower poly(Phe) synthesis but is more accurate than wild-type EF-Tu, probably due to a longer pausing on the ribosome.(ABSTRACT TRUNCATED AT 250 WORDS) ..
  81. Abrahams J, Kraal B, Bosch L. Zone-interference gel electrophoresis: a new method for studying weak protein-nucleic acid complexes under native equilibrium conditions. Nucleic Acids Res. 1988;16:10099-108 pubmed
    ..Studying the interactions between elongation factor EF-Tu and tRNA from E. coli we found for EF-Tu.GTP.aurodox.aminocyl-tRNA a Kd of 3 microM and for EF-Tu.GDP.aurodox.aminoacyl-tRNA a Kd of 11 microM at 9 degrees C. ..
  82. Andersen E, Rosenblad M, Larsen N, Westergaard J, Burks J, Wower I, et al. The tmRDB and SRPDB resources. Nucleic Acids Res. 2006;34:D163-8 pubmed publisher
    ..All alignments can be easily examined using a new exploratory browser. The databases provide links to high-resolution structures and serve as depositories for structures obtained by molecular modeling...
  83. Hammarlöf D, Hughes D. Mutants of the RNA-processing enzyme RNase E reverse the extreme slow-growth phenotype caused by a mutant translation factor EF-Tu. Mol Microbiol. 2008;70:1194-209 pubmed publisher
    ..Accordingly, RNase E is suggested to act at two distinct stages in the life of mRNA: early, on the nascent transcript; late, on the complete mRNA. ..
  84. Cool R, Jensen M, Jonak J, Clark B, Parmeggiani A. Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu. J Biol Chem. 1990;265:6744-9 pubmed
    ..These results are in agreement with the observations derived from x-ray diffraction analysis that the tertiary structure of the GTP-binding domain of elongation factor Tu and that of p21 are similar. ..
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    ..GDP labeled with [14C]TPCK revealed only one target site for this agent, i.e., cysteine-81. Modification occurred at the same site in the presence and in the absence of kirromycin and uncharged tRNA.(ABSTRACT TRUNCATED AT 250 WORDS) ..
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