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Genomes and Genes | tufBSummaryGene Symbol: tufB Description: protein chain elongation factor EF-Tu (duplicate of tufA) Alias: ECK3971, JW3943, kirT, pulT Species: Top Publications
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Publications
Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysisElizabeth Villa
Beckman Institute, University of Illinois at Urbana Champaign, Urbana, IL 61801, USA
Proc Natl Acad Sci U S A 106:1063-8. 2009..Our data suggest that GTP hydrolysis on EF-Tu is controlled through a hydrophobic gate mechanism...- Water induced effects on the thermal response of a proteinSimone Melchionna
Dipartimento di Fisica and INFM, Universita La Sapienza, Piazzale Aldo Moro 5, 00185 Rome, Italy
Phys Rev Lett 92:158101. 2004..The results support the notion that the dynamics of vicinal water makes a substantial contribution to the activity optimum of proteins... - Determination of the kinetics of guanine nucleotide exchange on EF-Tu and EF-Ts: continuing uncertaintiesKeith L Manchester
School of Molecular and Cell Biology, University of the Witwatersrand, Johannesburg, South Africa
Biochem Biophys Res Commun 314:1-5. 2004..Metabolic control analysis has been applied to determine the degree of flux control of the different steps in the pathway... - Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric formsHana Sanderová
Department of Protein Biosynthesis, Institute of Molecular Genetics, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Prague 6, Czech Republic
Protein Sci 13:89-99. 2004..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... - Regulation of translation of the head protein of T4 bacteriophage by specific binding of EF-Tu to a leader sequenceLarry Snyder
Department of Microbiology and Molecular Genetics, Michigan State University, East Lansing, MI 48824 4320, USA
J Mol Biol 334:349-61. 2003.... - Effects of mutagenesis of Gln97 in the switch II region of Escherichia coli elongation factor Tu on its interaction with guanine nucleotides, elongation factor Ts, and aminoacyl-tRNATomas Navratil
Department of Chemistry, Campus Box 3290, University of North Carolina, Chapel Hill, North Carolina 27599 3290, USA
Biochemistry 42:13587-95. 2003..Strikingly, the Q97P variant was completely inactive in ternary complex formation, accounting for its inability to function in polymerization. The structural basis of these observations is discussed... - Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopyMikel Valle
Howard Hughes Medical Institute, Health Research, Inc at the Wadsworth Center, Empire State Plaza, Albany, New York 12201 0509, USA
Nat Struct Biol 10:899-906. 2003..From these new findings we propose a mechanism that can explain the sequence of events during the decoding of mRNA on the ribosome... - Essential role of histidine 84 in elongation factor Tu for the chemical step of GTP hydrolysis on the ribosomeTina Daviter
Institute of Physical Biochemistry, University of Witten Herdecke, Stockumer Strasse 10, 58448, Witten, Germany
J Mol Biol 332:689-99. 2003..We propose that the catalytic role of His84 is to stabilize the transition state of GTP hydrolysis by hydrogen bonding to the attacking water molecule or, possibly, the gamma-phosphate group of GTP... - Functional EF-Tu with large C-terminal extensions in an E coli strain with a precise deletion of both chromosomal tuf genesRobert Schnell
Department of Microbiology, Stockholm University, S 106 91 Stockholm, Sweden
FEBS Lett 538:139-44. 2003..coli strain was constructed in which both chromosomal genes encoding elongation factor (EF)-Tu (tufA and tufB) have been inactivated with precise coding sequence replacements... - Specificity of elongation factor EF-TU for hydrophobic peptidesAbdelharim Malki
Stress Molecules, Institut Jacques Monod, Universite Paris 7, 2 place Jussieu, 75251 Paris Cedex 05, France
Biochem Biophys Res Commun 296:749-54. 2002..Our results suggest that EF-Tu, like DnaK, interacts albeit more weakly with the hydrophobic regions of substrate protein and are consistent with the hypothesis that it possesses chaperone properties... - Mechanism of elongation factor (EF)-Ts-catalyzed nucleotide exchange in EF-Tu. Contribution of contacts at the guanine baseHans Joachim Wieden
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
J Biol Chem 277:6032-6. 2002.... - Evolution of a molecular switch: universal bacterial GTPases regulate ribosome functionC E Caldon
School of Microbiology and Immunology, The University of New South Wales, Sydney, Australia
Mol Microbiol 41:289-97. 2001..If this is the case, then a corollary of this hypothesis is that GTPases that do not bind RNA arose at a later time from an RNA-binding progenitor that lost the capability to bind RNA... - Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-TuS E Heffron
Department of Physiology, University of California, Irvine 92697 4560, USA
Biochemistry 39:37-45. 2000..The results presented here provide the details necessary to enhance the solubility of GE2270A without disrupting its inhibitory properties... - Elongation factor Tu and DnaK are transferred from the cytoplasm to the periplasm of Escherichia coli during osmotic downshock presumably via the mechanosensitive channel mscLC Berrier
Laboratoire des Biomembranes, UMR CNRS 8619, Universite Paris Sud, 91405 Orsay Cedex, France
J Bacteriol 182:248-51. 2000..Release of these proteins is not observed in the absence of a Tris-EDTA treatment which disrupts the outer membrane, indicating that, in intact cells, they are transferred to the periplasm upon shock, presumably through the MscL channel... - Purification of elongation factors EF-Tu and EF-G from Escherichia coli by covalent chromatography on thiol-sepharoseT D Caldas
Biochimie Génétique, Institut Jacques Monod, Universite Paris 7, 2 place Jussieu, Paris Cedex 05, 75251, France
Protein Expr Purif 14:65-70. 1998..The specific reactivities of the elongation factors with thiol-Sepharose allow their efficient purification and suggest that they possess hitherto undiscovered properties connected with their reactive thiols... - Mutagenesis of glutamine 290 in Escherichia coli and mitochondrial elongation factor Tu affects interactions with mitochondrial aminoacyl-tRNAs and GTPase activitySenyene Eyo Hunter
Department of Chemistry, University of North Carolina, Campus Box 3290, Chapel Hill, North Carolina 27599 3290, USA
Biochemistry 43:6917-27. 2004..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... - Substrate-assisted catalysis of peptide bond formation by the ribosomeJoshua S Weinger
Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, Connecticut 06520 8114, USA
Nat Struct Mol Biol 11:1101-6. 2004..These results suggest that substrate assistance has been retained as a catalytic strategy during the evolution of the prebiotic peptidyl transferase center into the modern ribosome... - Mutants of the RNA-processing enzyme RNase E reverse the extreme slow-growth phenotype caused by a mutant translation factor EF-TuDisa L Hammarlöf
Microbiology Programme, Department of Cell and Molecular Biology, Uppsala University, Uppsala, Sweden
Mol Microbiol 70:1194-209. 2008..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... - Conserved discrimination against misacylated tRNAs by two mesophilic elongation factor Tu orthologsTerry J T Cathopoulis
Department of Chemistry, Johns Hopkins University, 3400 North Charles Street, Baltimore, Maryland 21218, USA
Biochemistry 47:7610-6. 2008..These results also demonstrate that the capacity of EF-Tu to discriminate against both of these aminoacyl-tRNAs is conserved even in bacteria like E. coli that do not generate either misacylated tRNA... - Elongation factor Tu mutants expand amino acid tolerance of protein biosynthesis systemYoshio Doi
Department of Bioscience and Biotechnology, Okayama University, Okayama, Japan
J Am Chem Soc 129:14458-62. 2007..L-1-Pyrenylalanine, L-2-pyrenylalanine, and DL-2-anthraquinonylalanine, which are hardly or only slightly incorporated with the wild-type EF-Tu, were successfully incorporated into a protein using these EF-Tu mutants... - Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteinsNicolas Brandes
Department of Molecular, Cellular and Developmental Biology, University of Michigan, Ann Arbor, MI, USA
Mol Microbiol 66:901-14. 2007..In vivo and in vitro activity studies confirmed that glutamate synthase rapidly inactivates upon NO treatment but is resistant towards other oxidative stressors... - The 51-63 base pair of tRNA confers specificity for binding by EF-TuLee E Sanderson
Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA
RNA 13:835-40. 2007..While this contact is an important specificity determinant, it is clear that others remain to be identified... - Molecular complementarity between tetracycline and the GTPase active site of elongation factor TuSusan E Heffron
Department of Physiology and Biophysics, 346 D Med Sci I, University of California, Irvine, CA 92697 4560, USA
Acta Crystallogr D Biol Crystallogr 62:1392-400. 2006.... - Probing the adaptive response of Escherichia coli to extracellular Zn(II)Tara K Sigdel
Department of Chemistry and Biochemistry, Miami University, 112 Hughes Hall, Oxford, OH 45056, USA
Biometals 19:461-71. 2006..coli proteins, and the results are discussed in light of recent genomic profiling studies on the adaptive response of E. coli cells to stress by Zn(II) excess... - Functional Qbeta replicase genetically fusing essential subunits EF-Ts and EF-Tu with beta-subunitHiroshi Kita
Department of Biotechnology, Graduate School of Engineering, Osaka University, Suita, Japan
J Biosci Bioeng 101:421-6. 2006..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... - The tmRDB and SRPDB resourcesEbbe Sloth Andersen
Department of Molecular Biology, University of Aarhus, C F Moellers Alle, Building 139, 8000 Aarhus, Denmark
Nucleic Acids Res 34:D163-8. 2006..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... - Opposite roles of domains 2+3 of Escherichia coli EF-Tu and Bacillus stearothermophilus EF-Tu in the regulation of EF-Tu GTPase activityHana Sanderová
Department of Gene Expression, Institute of Molecular Genetics, Academy of Sciences of the Czech Republic, Flemingovo nam 2, 166 37 Prague 6, Czech Republic
Biochim Biophys Acta 1752:11-7. 2005..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... - Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activationMihaela Diaconu
Röntgenkristallographie, Max Planck Institut fur biophysikalische Chemie, Am Fassberg 11, D 37077 Gottingen, Germany
Cell 121:991-1004. 2005..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... - The identification of the determinants of the cyclic, sequential binding of elongation factors tu and g to the ribosomeHuijun Yu
Department of Biochemistry and Molecular Biology, The University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA
J Mol Biol 386:802-13. 2009.... - The role of an activating peptide in protease-mediated suicide of Escherichia coli K12Nikki A Copeland
Department of Biology, The University of York, Heslington, York YO10 5YW, UK
J Biol Chem 280:112-7. 2005..coli K-12 by Lit is a variant form of "cofactor-induced activation," a mechanism of protease activation that has only been documented previously in pathogen subversion of mammalian hemostasis cascades... - Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocationFrank Peske
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
J Mol Biol 343:1183-94. 2004.... - Protecting the neighborhood: extreme measuresS Gottesman
National Cancer Institute, Building 37, Room 2E18, Bethesda, MD 20892-4255, USA
Proc Natl Acad Sci U S A 95:2731-2. 1998 - Isolation of tRNA isoacceptors by affinity chromatography with immobilized elongation factor Tu from Escherichia coliG Chinali
Dipartimento de Medicina Clinica e Sperimentale, Facolta di Medicina e Chirurgia, Universita di Napoli Federico II, Italy
J Biochem Biophys Methods 34:1-10. 1997..kirromycin allowed the isolation of the aminoacylated tRNA from bulk tRNA. A rapid and nearly quantitative recovery of highly purified tRNA isoacceptors for various amino acids was obtained in one chromatographic step... - In vitro construction of the tufB-lacZ fusion: analysis of the regulatory mechanism of tufB promoterY Takebe
Mol Gen Genet 187:355-63. 1982To investigate the regulatory mechanism of the tufB operon, we have constructed plasmids in which the lac structural genes have been fused to the regulatory region and the 5'-coding sequence of the tufB gene... - The nucleotide sequence of the cloned tufA gene of Escherichia coliT Yokota
Gene 12:25-31. 1980..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... - Characterization of promoter-cloning plasmids: analysis of operon structure in the rif region of Escherichia coli and isolation of an enhanced internal promoter mutantG An
J Bacteriol 144:904-16. 1980..for ribonucleic acid polymerase subunit beta'; (v) a gene coding for unknown protein U, which is located between tufB and the rplKA operon, had its own promoter; (vi) the tufB gene was separated from all of the genes described above .. - The complete amino-acid sequence of elongation factor Tu from Escherichia coliM D Jones
Eur J Biochem 108:507-26. 1980..The lysine residue at positon 56, in the polypeptide chain is partly methylated. The C-terminal residue is a mixture of serine and glycine, and this was the only heterogeneity found in the EF-Tu preparation used in this study... - Location of the site of methylation in elongation factor TuR A Laursen
FEBS Lett 107:359-62. 1979 - Location of the tufB promoter of E. coli: cotranscription of tufB with four transfer RNA genesJ S Lee
Cell 25:251-8. 1981..genes for four transfer RNA species (thrU, tyrU, glyT and thrT) are positioned close to one another and near tufB, one of the structural genes for elongation factor Tu... - Refined structure of elongation factor EF-Tu from Escherichia coliM Kjeldgaard
Department of Chemistry, Aarhus University, Denmark
J Mol Biol 223:721-42. 1992..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... - A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory proteinY W Hwang
New York State Office of Mental Retardation and Developmental Disabilities, Staten Island, New York 10314
J Biol Chem 262:13081-5. 1987..Aspartic acid 138 is conserved in the homologous sequences of all GTP regulatory proteins. This mutation would allow one to specifically alter the nucleotide specificity of other GTP regulatory proteins... - Site-directed mutagenesis of the GDP binding domain of bacterial elongation factor TuY W Hwang
New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314
Arch Biochem Biophys 274:394-403. 1989.... - Elongation factor Tu: a molecular switch in protein biosynthesisA Weijland
SDI No 61840 du CNRS, Laboratoire de Biochimie, Ecole Polytechnique, Palaiseau, France
Mol Microbiol 6:683-8. 1992..The regulation of the expression of the two EF-Tu-encoding genes in E. coli, particularly that of tufB, has been shown to involve diverse mechanisms... - Mutagenesis of bacterial elongation factor Tu at lysine 136. A conserved amino acid in GTP regulatory proteinsY W Hwang
Molecular Biology Department, New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314
J Biol Chem 264:8304-9. 1989..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... - Potential binding sites of the trans-activator FIS are present upstream of all rRNA operons and of many but not all tRNA operonsH Verbeek
Department of Biochemistry, Leiden University, Gorleaus Laboratories, The Netherlands
Biochim Biophys Acta 1050:302-6. 1990..Accordingly, FIS binding to an upstream sequence of the metY(nusA) operon was found to be weaker than that to the UAS of the thrU(tufB) operon. No FIS binding sites were found upstream three tRNA operons. - Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor TuR H Cool
Laboratoire de Biochimie, Ecole Polytechnique, URA 240 du Centre National de la Recherche Scientifique, Palaiseau, France
J Biol Chem 265:6744-9. 1990..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... - The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequenceR A Laursen
J Biol Chem 256:8102-9. 1981..Structural features of the aminoacyl-tRNA binding site are discussed in the light of sequence and other chemical and biochemical data... - Transcription of the E. coli tufB gene: cotranscription with four tRNA genes and inhibition by guanosine-5'-diphosphate-3'-diphosphateA Miyajima
Mol Gen Genet 183:13-9. 1981The 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... - Regulation of the expression of tufA and tufB, the two genes coding for the elongation factor EF-Tu in Escherichia coliP H van der Meide
FEBS Lett 139:325-30. 1982 - The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosomeE Vorstenbosch
Leiden Institute of Chemistry, Department of Biochemistry, Leiden University, The Netherlands
EMBO J 15:6766-74. 1996..Increasing the Mg2+ concentration appears to overcome the inhibition by screening the negative charges... - Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coliJ M Guillon
Laboratoire de Biochimie, URA CNRS 1970, Ecole Polytechnique, F91128 Palaiseau Cedex, France
J Biol Chem 271:22321-5. 1996..M., Mechulam, Y., Schmitter, J.-M., Blanquet, S., and Fayat, G. (1992) J. Bacteriol. 174, 4294-4301... - Escherichia coli RNA polymerase binding and initiation of transcription on fragments of lambda rifd 18 DNA containing promoters for lambda genes and for rrnB, tufB, rplC,A, rplJ,L, and rpoB,C genesW E Taylor
Gene 6:331-65. 1979Promoters of genes for bacteriophage lambda and for Escherichia coli ribosomal RNA (rrnB), elongation factor Tu (tufB), ribosomal proteins L11 (rplK), L1 (rplA), L10 (rplJ), and L7/L12 (rplL), and RNA polymerase subunits beta (rpoB) and .. - Lambda transducing bacteriophage carrying deletions of the argCBH-rpoBC region of the Escherichia coli chromosomeT Linn
J Bacteriol 140:479-89. 1979..We thus extend and confirm knowledge of the organization of this part of the chromosome. The new phages are useful tools for studying the genes for the bacterial transcription and translation machinery... - The ribosome as affinity matrix': efficient purification scheme for translation factorsM C Ganoza
Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada
Biochimie 78:51-61. 1996..The procedure markedly simplifies the isolation, in homogeneous form, of all the non-ribosomal proteins required to reconstruct translation... - Antibiotic resistance mechanisms of mutant EF-Tu species in Escherichia coliB Kraal
Leiden Institute of Chemistry, Department of Biochemistry, Leiden University, The Netherlands
Biochem Cell Biol 73:1167-77. 1995..mutagenesis methods have yielded sets of purified mutant EF-Tu resistant to kirromycin (kirT) or pulvomycin (pulT)... - Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNAO Wiborg
Department of Chemistry, Aarhus University, Langelandsgade 140, 8000 Aarhus C, Denmark
J Biol Chem 271:20406-11. 1996..Their functional roles are discussed in relation to the structure of elongation factor Tu in complex with aminoacyl-tRNA... - The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolutionT Kawashima
European Molecular Biology Laboratory, Grenoble Outstation, France
Nature 379:511-8. 1996..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... - Prokaryotic elongation factor Tu is phosphorylated in vivoC Lippmann
Institut fur Biochemie, Freie Universitat Berlin, Germany
J Biol Chem 268:601-7. 1993..coli. Protein sequencing of both the in vivo and in vitro phosphorylated protein revealed position 382 as the modified threonine residue... - Mutants of Escherichia coli altered in both genes coding for the elongation factor TuJ A van de Klundert
Proc Natl Acad Sci U S A 75:4470-3. 1978..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... - The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coliJ R Mesters
Department of Biochemistry, Leiden University, The Netherlands
EMBO J 13:4877-85. 1994..The first inhibits access of the antibiotic to its binding site on EF-Tu.GTP. A second mechanism exists on the ribosome, when mutant EF-Tu species release kirromycin and polypeptide chain elongation continues... - Dual function transcripts specifying tRNA and mRNAL Hudson
Nature 294:422-7. 1981 - Elongation factor Tu is methylated in response to nutrient deprivation in Escherichia coliC C Young
Department of Molecular and Cell Biology, Pennsylvania State University, University Park 16802
J Bacteriol 173:3096-100. 1991..We propose that the nutrient-dependent methylation of EF-Tu may be involved in the regulation of growth, possibly as a principal component of an unidentified signal transduction pathway in bacteria... - Trans-translation: the tmRNA-mediated surveillance mechanism for ribosome rescue, directed protein degradation, and nonstop mRNA decayDaniel Dulebohn
Department of Biochemistry and Cell Biology and The Center for Infectious Diseases, Stony Brook University, Stony Brook, New York 11794, USA
Biochemistry 46:4681-93. 2007..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... - Mutational analysis of the roles of residues in Escherichia coli elongation factor Ts in the interaction with elongation factor TuY Zhang
Department of Chemistry, University of North Carolina, Chapel Hill, North Carolina 27599 3290, USA
J Biol Chem 273:4556-62. 1998..Mutations prepared in EF-Tu indicate that His-19 and Gln-114 but not Glu-348 in EF-Tu are moderately important for its interaction with EF-Ts... - Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolutionH Song
School of Biochemistry and Molecular Biology, University of Leeds, Leeds, LS2 9JT, UK
J Mol Biol 285:1245-56. 1999..Comparisons of the Mg2+ binding site with other guanine nucleotide binding proteins in GDP-bound forms show that the Mg2+ co-ordination patterns are well preserved among these structures... - Enacyloxin IIa pinpoints a binding pocket of elongation factor Tu for development of novel antibioticsAndrea Parmeggiani
Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10 C, DK 8000 Aarhus C, Denmark
J Biol Chem 281:2893-900. 2006..This work clarifies the structural background of the action of enacyloxin IIa and compares its properties with those of kirromycin, opening new perspectives for structure-guided design of novel antibiotics... - Single-molecule structural dynamics of EF-G--ribosome interaction during translocationYuhong Wang
Pennsylvania Muscle Institute, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104 6083, USA
Biochemistry 46:10767-75. 2007..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... - Transcription of the tRNA-tufB operon of Escherichia coli: activation, termination and antiterminationJ H van Delft
Department of Biochemistry, University of Leiden, The Netherlands
Nucleic Acids Res 15:9515-30. 1987Signals setting the level of transcription of the tRNA-tufB operon have been studied by deletion mapping. TufB transcription was measured in vivo with plasmid-borne tRNA-tufB:galk operon fusions... - Pulvomycin-resistant mutants of E.coli elongation factor TuL A Zeef
Department of Biochemistry, Leiden University, The Netherlands
EMBO J 13:5113-20. 1994..GTP conformation. Genetic and protein characterizations show that sensitivity to pulvomycin is dominant over resistance. This appears to contradict the currently accepted model of protein synthesis inhibition by pulvomycin... - Translational activities of EF-Tu [G222D] which cannot be reconciled with the classical scheme of the polypeptide chain elongation cycleA Talens
Department of Biochemistry, Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, The Netherlands
Biochem Biophys Res Commun 225:961-7. 1996..Vijgenboom, E., & Zeef, L.A.H., 1996, Biochemistry 36)... - An active role for tRNA in decoding beyond codon:anticodon pairingLuisa Cochella
Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
Science 308:1178-80. 2005..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...