Genomes and Genes
gtp phosphohydrolase linked elongation factors
Summary: Factors that utilize energy from the hydrolysis of GTP to GDP for peptide chain elongation. EC 3.6.1.-.
- Al Karadaghi S, Aevarsson A, Garber M, Zheltonosova J, Liljas A. The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange. Structure. 1996;4:555-65 pubmed..The conformation of EF-G-GDP around the nucleotide-binding site may be related to the mechanism of nucleotide exchange...
- Mistou M, Cool R, Parmeggiani A. Effects of ions on the intrinsic activities of c-H-ras protein p21. A comparison with elongation factor Tu. Eur J Biochem. 1992;204:179-85 pubmed..5-10, suggesting that the bell-shaped behaviour of this activity in the absence of the antibiotic is due to denaturation. This implies similar properties in the catalytic mechanism of these two guanine-nucleotide-binding proteins. ..
- Abel K, Yoder M, Hilgenfeld R, Jurnak F. An alpha to beta conformational switch in EF-Tu. Structure. 1996;4:1153-9 pubmed..The alpha to beta switch in EF-Tu may represent a prototypical activation mechanism for other protein families. ..
- Boriack Sjodin P, Margarit S, Bar Sagi D, Kuriyan J. The structural basis of the activation of Ras by Sos. Nature. 1998;394:337-43 pubmed..Sos does not impede the binding sites for the base and the ribose of GTP or GDP, so the Ras-Sos complex adopts a structure that allows nucleotide release and rebinding. ..
- Miyazaki M, Uritani M, Kagiyama H. The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes. J Biochem. 1988;104:445-50 pubmed..From experiments on protection against tryptic digestion, we determined that intricate conformational changes of the factor molecule occur upon interaction with the substrate XTP and ribosomes. ..
- Caldas T, El Yaagoubi A, Kohiyama M, Richarme G. Purification of elongation factors EF-Tu and EF-G from Escherichia coli by covalent chromatography on thiol-sepharose. Protein Expr Purif. 1998;14:65-70 pubmed..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. ..
- Lill R, Robertson J, Wintermeyer W. Binding of the 3' terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation. EMBO J. 1989;8:3933-8 pubmed..The co-operative interaction between the E site and the EF-G binding site, which are distantly located on the 50S ribosomal subunit, is probably mediated by a conformational change of 23S rRNA. ..
- 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. ..
- Zeidler W, Egle C, Ribeiro S, Wagner A, Katunin V, Kreutzer R, et al. Site-directed mutagenesis of Thermus thermophilus elongation factor Tu. Replacement of His85, Asp81 and Arg300. Eur J Biochem. 1995;229:596-604 pubmed..thermophilus EF-Tu. Mutation of His85, a residue which is not directly involved in the nucleotide binding, thus influences the interaction of EF-Tu domains, nucleotide binding and the efficiency and rate of GTPase activity. ..
- 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) ..
- Martemyanov K, Yarunin A, Liljas A, Gudkov A. An intact conformation at the tip of elongation factor G domain IV is functionally important. FEBS Lett. 1998;434:205-8 pubmed..It is concluded that the native conformation of the loop is important for the factor-promoted translocation in the ribosome. The functional importance of the entire EF-G domain IV is discussed...
- Kubarenko A, Sergiev P, Rodnina M. [GTPases of translational apparatus]. Mol Biol (Mosk). 2005;39:746-61 pubmed..This review is devoted to the functional peculiarities of translational GTPases as related to other G-proteins. Particularly, to the putative GTPase activation mechanism, structure and functional cycles. ..
- Rodnina M, Serebryanik A, Ovcharenko G, El skaya A. ATPase strongly bound to higher eukaryotic ribosomes. Eur J Biochem. 1994;225:305-10 pubmed..Rabbit liver ribosomes seem to stimulate the ATPase activity of yeast EF-3 similar to the mechanism in yeast ribosomes, though less efficiently. ..
- Dunkle J, Cate J. Ribosome structure and dynamics during translocation and termination. Annu Rev Biophys. 2010;39:227-44 pubmed publisher..Finally, we review recent advances in understanding how bacteria handle errors in both translocation and termination. ..
- 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. ..
- Rodnina M, Savelsbergh A, Matassova N, Katunin V, Semenkov Y, Wintermeyer W. Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome. Proc Natl Acad Sci U S A. 1999;96:9586-90 pubmed..The results indicate that thiostrepton inhibits a structural transition of the 1067 region of 23S rRNA that is important for functions of EF-G after GTP hydrolysis. ..
- Vorstenbosch E, Pape T, Rodnina M, Kraal B, Wintermeyer W. The G222D mutation in elongation factor Tu inhibits the codon-induced conformational changes leading to GTPase activation on the ribosome. EMBO J. 1996;15:6766-74 pubmed..Increasing the Mg2+ concentration appears to overcome the inhibition by screening the negative charges. ..
- Martemyanov K, Liljas A, Gudkov A. Increased functional activity of elongation factor G with G16V mutation in the GTP-binding domain. Biochemistry (Mosc). 1998;63:1216-9 pubmed..coli. The mutated protein with an uncleavable GTP analog also has an increased affinity to the ribosomes. ..
- Bilgin N, Claesens F, Pahverk H, Ehrenberg M. Kinetic properties of Escherichia coli ribosomes with altered forms of S12. J Mol Biol. 1992;224:1011-27 pubmed..We use our in vitro findings to discuss the in vivo physiology of these mutants as well as mechanistic features of E. coli translation. ..
- Krab I, Parmeggiani A. Functional-structural analysis of threonine 25, a residue coordinating the nucleotide-bound magnesium in elongation factor Tu. J Biol Chem. 1999;274:11132-8 pubmed..They emphasize the importance of the Thr-25-Mg2+ bond, although its absence is compatible with protein synthesis and thus with an active overall conformation of EF-Tu. ..
- Zeef L, Mesters J, Kraal B, Bosch L. A growth-defective kirromycin-resistant EF-Tu Escherichia coli mutant and a spontaneously evolved suppression of the defect. Gene. 1995;165:39-43 pubmed..We also show that strains containing the segregated tufA Q124K mutation formed filaments. ..
- Masullo M, De Vendittis E, Bocchini V. Archaebacterial elongation factor 1 alpha carries the catalytic site for GTP hydrolysis. J Biol Chem. 1994;269:20376-9 pubmed..A molecular mechanism for this activation is proposed. ..
- March P. Membrane-associated GTPases in bacteria. Mol Microbiol. 1992;6:1253-7 pubmed..In spite of similarities to well-studied eukaryotic proteins the signalling pathways of these cellular regulators, with the exception of NodQ, have not yet been elucidated. ..
- Ahmadian M, Kreutzer R, Blechschmidt B, Sprinzl M. Site-directed mutagenesis of Thermus thermophilus EF-Tu: the substitution of threonine-62 by serine or alanine. FEBS Lett. 1995;377:253-7 pubmed..GTP. These observations are in agreement with the tertiary structure of EF-Tu.GTP, in which threonine-62 is interacting with the Mg2+ ion, gamma-phosphate of GTP and a water molecule, which is presumably involved in the GTP hydrolysis. ..
- Swart G, Parmeggiani A. tRNA and the guanosinetriphosphatase activity of elongation factor Tu. Biochemistry. 1989;28:327-32 pubmed..When EF-Tu acts as a component of the ternary complex formed with GTP and aa-tRNA, the presence of tRNA in the P-site strongly increases the GTPase activity.(ABSTRACT TRUNCATED AT 250 WORDS) ..
- Hou Y, Yaskowiak E, March P. Carboxyl-terminal amino acid residues in elongation factor G essential for ribosome association and translocation. J Bacteriol. 1994;176:7038-44 pubmed..We propose that all of these mutations are present in a domain that is essential for ribosome association and that GTP hydrolysis was deficient as a secondary consequence of impaired binding to 70S ribosomes. ..
- Laalami S, Grentzmann G, Bremaud L, Cenatiempo Y. Messenger RNA translation in prokaryotes: GTPase centers associated with translational factors. Biochimie. 1996;78:577-89 pubmed..Of the prokaryotic translational factors, IF2, EF-Tu, SELB, EF-G and RF3 are GTP-binding proteins. In this review we summarize the latest findings on the structures and the roles of these GTPases in the translational process. ..
- Jacquet E, Parmeggiani A. Substitution of Val20 by Gly in elongation factor Tu. Effects on the interaction with elongation factors Ts, aminoacyl-tRNA and ribosomes. Eur J Biochem. 1989;185:341-6 pubmed..mRNA, as a consequence of a longer pausing of EF-TuG20 on the ribosome. In conclusion, position 20 in EF-Tu is important for coordinating the allosteric mechanisms controlling the action of EF-Tu and its ligands. ..
- Mesters J, Martien de Graaf J, Kraal B. Divergent effects of fluoroaluminates on the peptide chain elongation factors EF-Tu and EF-G as members of the GTPase superfamily. FEBS Lett. 1993;321:149-52 pubmed..Interestingly, in the absence of ribosomes both EF-Tu an EF-G remain totally unaffected by fluoraluminates. For members of the GTPase superfamily such differential effects have not been described before. ..
- Keeling P, Fast N, McFadden G. Evolutionary relationship between translation initiation factor eIF-2gamma and selenocysteine-specific elongation factor SELB: change of function in translation factors. J Mol Evol. 1998;47:649-55 pubmed..The overall topology of the GTPase tree further suggests that the eIF-2gamma/SELB group may represent an ancient subfamily of GTPases that diverged prior to the last common ancestor of extant life. ..
- Pedersen G, Rattenborg T, Knudsen C, Clark B. The role of Glu259 in Escherichia coli elongation factor Tu in ternary complex formation. Protein Eng. 1998;11:101-8 pubmed
- Cetin R, Anborgh P, Cool R, Parmeggiani A. Functional role of the noncatalytic domains of elongation factor Tu in the interactions with ligands. Biochemistry. 1998;37:486-95 pubmed
- Nagel K, Voigt J. An inhibitor of elongation factor G (EF-G) GTPase present in the ribosome wash of Escherichia coli: a complex of initiation factors IF1 and IF3?. Biochim Biophys Acta. 1992;1129:145-8 pubmed..Therefore, IF1 as well as the EF-G GTPase inhibitor do not influence the ribosome-dependent EF-G GTPase by affecting the association of ribosomal subunits. ..
- Grentzmann G, Kelly P, Laalami S, Shuda M, Firpo M, Cenatiempo Y, et al. Release factor RF-3 GTPase activity acts in disassembly of the ribosome termination complex. RNA. 1998;4:973-83 pubmed..Based on our results, we propose a model of how RF3 might function in translational termination and ribosome recycling. ..
- Burdett V. Tet(M)-promoted release of tetracycline from ribosomes is GTP dependent. J Bacteriol. 1996;178:3246-51 pubmed..Furthermore, while Tet(M) protects translation from tetracycline inhibition in a defined system, it is unable to substitute for either EF-G or elongation factor Tu. ..
- Kinzy T, Merrick W. Characterization of a limited trypsin digestion form of eukaryotic elongation factor 1 alpha. J Biol Chem. 1991;266:4099-105 pubmed..Limited trypsin digestion of modified protein indicates that none of these reagents cross-links GTP to the first 69 amino acids of EF-1 alpha, which includes the first GTP binding consensus element, GXXXXGK. ..
- Chinali G, Vanlinden F, Cocito C. Action of virginiamycin M on the stability of different ribosomal complexes to ultracentrifugation. Biochim Biophys Acta. 1988;950:67-74 pubmed..This interpretation is supported by the finding that the ribosome-promoted protection of aminoacyl-tRNA against spontaneous hydrolysis is suppressed by virginiamycin M. ..
- Ganoza M, Cunningham C, Green R. A new factor from Escherichia coli affects translocation of mRNA. J Biol Chem. 1995;270:26377-81 pubmed..We propose that W functions by ejecting tRNAs from ribosomes in a step that precedes the movement of mRNA during translocation. ..
- Andersen C, Wiborg O. Escherichia coli elongation-factor-Tu mutants with decreased affinity for aminoacyl-tRNA. Eur J Biochem. 1994;220:739-44 pubmed..The Kd is about 20-times higher for H66A compared to wild type. Our results strongly suggest that His66 and His118 play major roles in stabilization of the ternary complex. ..
- Pape T, Wintermeyer W, Rodnina M. Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome. EMBO J. 1999;18:3800-7 pubmed..As kinetically favored incorporation of the correct substrate has also been suggested for DNA and RNA polymerases, the present findings indicate that induced fit may contribute to the fidelity of template-programed systems in general. ..
- 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...
- Rodnina M, Savelsbergh A, Katunin V, Wintermeyer W. Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature. 1997;385:37-41 pubmed..By coupling the free energy of GTP hydrolysis to translocation, EF-G serves as a motor protein to drive the directional movement of transfer and messenger RNAs on the ribosome. ..
- Jensen M, Cool R, Mortensen K, Clark B, Parmeggiani A. Structure-function relationships of elongation factor Tu. Isolation and activity of the guanine-nucleotide-binding domain. Eur J Biochem. 1989;182:247-55 pubmed..The inability of the G domain to sustain poly(Phe) synthesis is in agreement with the apparent lack of formation of a ternary complex between the G domain.GTP complex and aa-tRNA.(ABSTRACT TRUNCATED AT 400 WORDS) ..
- Raimo G, Masullo M, Scarano G, Bocchini V. The site for GTP hydrolysis on the archaeal elongation factor 2 is unmasked by aliphatic alcohols. Biochimie. 1996;78:832-7 pubmed..The stimulatory effect of ethylene glycol/Ba2+ was attributed to the increased affinity for GTP, probably related to a conformational change occurring in a hydrophobic region near the catalytic site. ..
- Thompson J, Musters W, Cundliffe E, Dahlberg A. Replacement of the L11 binding region within E.coli 23S ribosomal RNA with its homologue from yeast: in vivo and in vitro analysis of hybrid ribosomes altered in the GTPase centre. EMBO J. 1993;12:1499-504 pubmed..coli and yeast rRNAs allows the hybrid ribosomes to function competently in protein synthesis and also preserves the interaction with thiostrepton. ..
- Ogasawara T, Ito K, Igarashi K, Yutsudo T, Nakabayashi N, Takeda Y. Inhibition of protein synthesis by a Vero toxin (VT2 or Shiga-like toxin II) produced by Escherichia coli O157:H7 at the level of elongation factor 1-dependent aminoacyl-tRNA binding to ribosomes. Microb Pathog. 1988;4:127-35 pubmed..VT2 did not affect Met-tRNAf binding to ribosomes, non-enzymatic binding of aminoacyl-tRNA to ribosomes, peptide bond formation or translocation. ..
- Miyazaki M, Kagiyama H. Soluble factor requirements for the Tetrahymena peptide elongation system and the ribosomal ATPase as a counterpart of yeast elongation factor 3 (EF-3). J Biochem. 1990;108:1001-8 pubmed..It was also shown that the ribosomal nucleotidase plays a pivotal role in the elongation cycle in other eukaryotes. ..
- Laurberg M, Mansilla F, Clark B, Knudsen C. Investigation of functional aspects of the N-terminal region of elongation factor Tu from Escherichia coli using a protein engineering approach. J Biol Chem. 1998;273:4387-91 pubmed
- Weijland A, Parmeggiani A. Toward a model for the interaction between elongation factor Tu and the ribosome. Science. 1993;259:1311-4 pubmed..This stoichiometry of two is associated with the binding of the correct aa-tRNA to the ribosome. ..
- Hall C, Watkins J, Georgopapadakou N. Effects of elfamycins on elongation factor Tu from Escherichia coli and Staphylococcus aureus. Antimicrob Agents Chemother. 1989;33:322-5 pubmed..13 microM. This suggests that the observed high MICs of kirromycin and its congeners in S. aureus reflect a kirromycin-resistant EF-Tu rather than permeability constraints. ..
- Kahns S, Lund A, Kristensen P, Knudsen C, Clark B, Cavallius J, et al. The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res. 1998;26:1884-90 pubmed..In contrast, the GDP dissociation rate constant is approximately 7 times higher for eEF1A-1 than for eEF1A-2. The nucleotide preference ratio (GDP/GTP) for eEF1A-1 was 0.82, while the preference ratio for eEF1A-2 was 1.50. ..
- Masullo M, Ianniciello G, Arcari P, Bocchini V. Properties of truncated forms of the elongation factor 1alpha from the archaeon Sulfolobus solfataricus. Eur J Biochem. 1997;243:468-73 pubmed
- Rattenborg T, Nautrup Pedersen G, Clark B, Knudsen C. Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality. Eur J Biochem. 1997;249:408-14 pubmed..However, the mutants' abilities to bind aminoacyl-tRNA and protect the labile aminoacyl bond were impaired, especially where the charge had been reversed. ..