Research Topics
| M V RodninaSummaryAffiliation: University of Witten/Herdecke Country: Germany Publications
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Detail Information
Publications
Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosomeBerthold Wilden
Institutes of Molecular Biology and Physical Biochemistry, University of Witten-Herdecke, D-58448 Witten, Germany
Proc Natl Acad Sci U S A 103:13670-5. 2006..GTP hydrolysis is required for rapid tRNA-mRNA movement, and P(i) release induces further rearrangements of both EF-G and the ribosome that are required for EF-G turnover...
Conservation of bacterial protein synthesis machinery: initiation and elongation in Mycobacterium smegmatisChristian M Bruell
Institute of Medical Microbiology, University of Zurich, Switzerland
Biochemistry 47:8828-39. 2008..smegmatis components as an alternative to that from E. coli to study the mechanisms of translation and to test the action of antibiotics against Gram-positive bacteria...
[Mechanism of tRNA translocation on the ribosome]M V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Mol Biol (Mosk) 35:655-65. 2001....- Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanismsM V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Annu Rev Biochem 70:415-35. 2001..In utilizing induced fit for substrate discrimination, the ribosome resembles other nucleic acid-programmed polymerases... - The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocationMarina V Rodnina
Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
Biochem Soc Trans 39:658-62. 2011..EF-G acts as a Brownian ratchet providing directional bias for movement at the cost of GTP hydrolysis... - Ribosome fidelity: tRNA discrimination, proofreading and induced fitM V Rodnina
Institutes of Physical Biochemistry and Molecular Biology, University of Witten Herdecke, 58448, Witten, Germany
Trends Biochem Sci 26:124-30. 2001..Similar mechanisms are used by other template-programmed enzymes, such as DNA and RNA polymerases... - How ribosomes make peptide bondsMarina V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, D 58448 Witten, Germany
Trends Biochem Sci 32:20-6. 2007..Proton transfer during the reaction seems to be promoted by a concerted shuttle mechanism that involves ribose hydroxyl groups on the tRNA substrate... - Mechanism of peptide bond formation on the ribosomeMarina V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, Witten, Germany
Q Rev Biophys 39:203-25. 2006..The catalytic mechanism employed by the ribosome suggests how ancient RNA-world enzymes may have functioned... - Structural dynamics of ribosomal RNA during decoding on the ribosomeMarina V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, Stockumer Str 10, 58448, Witten, Germany
Biochimie 84:745-54. 2002.... - Peptide bond formation on the ribosome: structure and mechanismMarina V Rodnina
Institutes of Physical Biochemistry and Molecular Biology, University of Witten Herdecke, Stockumer Strasse 10, 58448, Witten, Germany
Curr Opin Struct Biol 13:334-40. 2003..According to the kinetics of mutant ribosomes, these effects may be attributed to a candidate catalytic base (A2451) suggested by the crystal structure... - Ten remarks on peptide bond formation on the ribosomeM V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Biochem Soc Trans 33:493-8. 2005..10(7)-fold rate enhancement of peptide bond formation by the ribosome is mainly due to substrate positioning within the active site, rather than to chemical catalysis... - Important role of the tetraloop region of 4.5S RNA in SRP binding to its receptor FtsYJ R Jagath
Institute of Molecular Biology, University of Witten Herdecke, Witten, Germany
RNA 7:293-301. 2001.... - Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosomeM V Rodnina
Institute of Molecular Biology, University of Witten Herdecke, Germany
Nature 385:37-41. 1997..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... - Mechanisms of elongation on the ribosome: dynamics of a macromolecular machineW Wintermeyer
Institute of Molecular Biology, University of Witten Herdecke, Stockumer Str 10, 58448 Witten, Germany
Biochem Soc Trans 32:733-7. 2004..This review summarizes recent progress in understanding the mechanisms of the elongation phase of protein synthesis. Results from rapid kinetic analysis of elongation reactions are discussed in the light of recent structural data... - Ribosomal RNA is the target for oxazolidinones, a novel class of translational inhibitorsN B Matassova
Institute of Molecular Biology, University of Witten Herdecke, Witten, Germany
RNA 5:939-46. 1999..Both binding sites and mode of action of oxazolidinones are unique among the antibiotics known to act on the ribosome... - GTPases mechanisms and functions of translation factors on the ribosomeM V Rodnina
Institute of Molecular Biology, University of Witten Herdecke, Germany
Biol Chem 381:377-87. 2000..GTP hydrolysis by IF2 is triggered upon formation of the 70S initiation complex, and the dissociation of Pi and/or IF2 follows a rearrangement of the ribosome into the elongation-competent state... - Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12A Savelsbergh
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
J Biol Chem 275:890-4. 2000..L7/12 appears to function by stabilizing the GTPase transition state of EF-G... - Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosomeM V Rodnina
Institute of Molecular Biology, University of Witten Herdecke, D 58448 Witten, Germany
Proc Natl Acad Sci U S A 96:9586-90. 1999..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... - Essential mechanisms in the catalysis of peptide bond formation on the ribosomeMalte Beringer
Institute of Physical Biochemistry, University of Witten/Herdecke, Stockumer Strasse 10, 58448 Witten, Germany
J Biol Chem 280:36065-72. 2005..A2451 seems to function as a pivot point in ordering the structure of the peptidyl transferase center rather than taking part in chemical catalysis... - Modulation of the rate of peptidyl transfer on the ribosome by the nature of substratesIngo Wohlgemuth
Institute of Physical Biochemistry, University of Witten Herdecke, Stockumer Strasse 10, D 58448 Witten, Germany
J Biol Chem 283:32229-35. 2008..On the other hand, the 50-fold increase in the reaction rate for peptidyl-tRNA ending with Pro suggests that full-length aminoacyl-tRNA in the A site greatly accelerates peptide bond formation... - The ribosome's response to codon-anticodon mismatchesT Daviter
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany
Biochimie 88:1001-11. 2006..This review emphasizes the progress made in understanding the mechanisms that determine recognition and selection of tRNA by the translational machinery... - Kinetic determinants of high-fidelity tRNA discrimination on the ribosomeKirill B Gromadski
Institute of Physical Biochemistry, University of Witten/Herdecke, D-58448 Witten, Germany
Mol Cell 13:191-200. 2004..tRNA selection at the initial selection step is entirely kinetically controlled and is due to much faster (650-fold) GTP hydrolysis of cognate compared to near-cognate substrate... - A common structural motif in elongation factor Ts and ribosomal protein L7/12 may be involved in the interaction with elongation factor TuH J Wieden
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany
J Mol Evol 52:129-36. 2001..The motif is remarkably similar with respect to fold, bulkiness, and charge distribution of the solution surface, suggesting that it has a common function in binding EF-Tu... - 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... - Peptide bond formation does not involve acid-base catalysis by ribosomal residuesPeter Bieling
Institute of Physical Biochemistry, University of Witten/Herdecke, Stockumer Strasse 10, 58448 Witten, Germany
Nat Struct Mol Biol 13:423-8. 2006..The rate of peptide bond formation with unmodified Phe-tRNA(Phe) is estimated to be >300 s(-1)... - The ribosomal peptidyl transferaseMalte Beringer
Institute of Physical Biochemistry, University of Witten Herdecke, Witten, Germany
Mol Cell 26:311-21. 2007..Proton transfer during the reaction appears to be promoted by a concerted proton shuttle mechanism that involves ribose hydroxyl groups on the tRNA substrate... - Interaction of guanine nucleotides with the signal recognition particle from Escherichia coliJ R Jagath
Institute of Molecular Biology, University of Witten Herdecke, Germany
Biochemistry 37:15408-13. 1998..Binding of both GTP and GDP to Ffh was independent of Mg2+ ions. The data suggest that, at conditions in vivo, (i) there will be rapid spontaneous GDP-GTP exchange, and (ii) the GTP-bound form of Ffh, or of SRP, will be predominant... - Control of phosphate release from elongation factor G by ribosomal protein L7/12Andreas Savelsbergh
Institute of Molecular Biology, University of Witten Herdecke, Witten, Germany
EMBO J 24:4316-23. 2005.... - A uniform response to mismatches in codon-anticodon complexes ensures ribosomal fidelityKirill B Gromadski
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany
Mol Cell 21:369-77. 2006..The forward reactions on mismatched codons were particularly sensitive to the disruption of the A-minor interactions with 16S rRNA and determined the variations in the misreading efficiency of near-cognate codons... - Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelBAlena Paleskava
Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
J Biol Chem 285:3014-20. 2010..The mode of tRNA recognition by SelB is reminiscent of another specialized factor, eIF2, rather than of EF-Tu, the common delivery factor for all other aminoacyl-tRNAs, in line with a common evolutionary ancestry of SelB and eIF2... - Truncated elongation factor G lacking the G domain promotes translocation of the 3' end but not of the anticodon domain of peptidyl-tRNAC Borowski
Institute of Molecular Biology, University of Witten Herdecke, Germany
Proc Natl Acad Sci U S A 93:4202-6. 1996..The G domain's intramolecular interactions are likely to be modulated by GTP binding and hydrolysis... - Delayed release of inorganic phosphate from elongation factor Tu following GTP hydrolysis on the ribosomeUte Kothe
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Biochemistry 45:12767-74. 2006..Rather, the slow P(i) release may be a consequence of the tight interaction of the switch regions of EF-Tu with the gamma-phosphate and the ribosome in the GTPase activated state of the factor... - GTPase activation of elongation factors Tu and G on the ribosomeDagmar Mohr
Institute of Physical Biochemistry, University of Witten/Herdecke, Stockumer Strasse 10, D-58448 Witten, Germany
Biochemistry 41:12520-8. 2002..This effect appears to be augmented by interactions of other structural elements of the large ribosomal subunit with the switch regions of the factors... - The signal recognition particle binds to protein L23 at the peptide exit of the Escherichia coli ribosomeShan Qing Gu
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
RNA 9:566-73. 2003..These results indicate a model of the topographical arrangement of SRP at the peptide exit of the 50S ribosomal subunit... - Conformation of 4.5S RNA in the signal recognition particle and on the 30S ribosomal subunitShan Qing Gu
Institute of Molecular Biology, University of Witten Herdecke, Stockumer Str 10, 58448 Witten, Germany
RNA 11:1374-84. 2005..The functional role of 4.5S RNA binding to the 30S subunit is unclear, as the RNA had no effect on translation or tRNA translocation on the ribosome... - Sequence of steps in ribosome recycling as defined by kinetic analysisFrank Peske
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
Mol Cell 18:403-12. 2005..IF3 is required for the subsequent ejection of tRNA and mRNA from the small subunit. The latter step is slower than subunit dissociation and constitutes the rate-limiting step of ribosome recycling... - Rapid peptide bond formation on isolated 50S ribosomal subunitsIngo Wohlgemuth
Institute of Physical Biochemistry, University of Witten/Herdecke, Stockumer Strasse 10, 58448 Witten, Germany
EMBO Rep 7:699-703. 2006.... - Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complexHolger Stark
Max Planck Institute for Biophysical Chemistry, 37077 Gottingen, Germany
Nat Struct Biol 9:849-54. 2002..These results provide a detailed snapshot view of an important functional state of the ribosome and suggest mechanisms of decoding and GTPase activation... - Optimization of speed and accuracy of decoding in translationIngo Wohlgemuth
Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Gottingen, Germany
EMBO J 29:3701-9. 2010..The GTP hydrolysis step is crucial for the optimization of both the speed and accuracy, which explains the necessity for the trade-off between the two fundamental parameters of translation... - Ribosome dynamics and tRNA movement by time-resolved electron cryomicroscopyNiels Fischer
3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Gottingen, Germany
Nature 466:329-33. 2010..The ribosome functions as a Brownian machine that couples spontaneous conformational changes driven by thermal energy to directed movement... - Codon reading by tRNAAla with modified uridine in the wobble positionUte Kothe
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Mol Cell 25:167-74. 2007..g., the GCC codon. The ribosome accepts the C-cmo(5)U pair as an almost-correct base pair, unlike third-position mismatches, which lead to the incorporation of incorrect amino acids and are efficiently rejected... - Recognition and selection of tRNA in translationMarina V Rodnina
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
FEBS Lett 579:938-42. 2005..Recent results of kinetic measurements, ribosome crystallography, single molecule FRET measurements, and cryo-electron microscopy suggest the mechanism of tRNA recognition and selection... - 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.... - Conformation of the signal recognition particle in ribosomal targeting complexesIwona A Buskiewicz
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
RNA 15:44-54. 2009..Binding of FtsY to the RNC-SRP complex results in a limited conformational change of SRP, which may initiate subsequent targeting steps... - Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosomeKirill B Gromadski
Institute of Physical Biochemistry, University of Witten/Herdecke, D-58448 Witten, Germany
Nat Struct Mol Biol 11:316-22. 2004..These results indicate that movements within the 30S subunit at the streptomycin-binding site are essential for the coupling between base pair recognition and GTP hydrolysis, thus modulating the fidelity of aa-tRNA selection... - 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.... - Interaction of helix D of elongation factor Tu with helices 4 and 5 of protein L7/12 on the ribosomeUte Kothe
Institute of Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany
J Mol Biol 336:1011-21. 2004..By analogy to the interaction of helix D of EF-Tu with the N-terminal domain of EF-Ts, the contact area is likely to consist of a hydrophobic patch flanked by two salt-bridges... - Importance of tRNA interactions with 23S rRNA for peptide bond formation on the ribosome: studies with substrate analogsMalte Beringer
Institute of Physical Biochemistry, University of Witten Herdecke, Witten, Germany
Biol Chem 388:687-91. 2007..The tRNA-rRNA interactions lead to a robust reaction that is insensitive to pH changes or base substitutions in 23S rRNA at the active site of the ribosome... - Spontaneous reverse movement of mRNA-bound tRNA through the ribosomeAndrey L Konevega
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
Nat Struct Mol Biol 14:318-24. 2007..These results lend support to the diffusion model of tRNA movement during translocation. In the cell, tRNA movement is biased in the forward direction by EF-G, which acts as a Brownian ratchet and prevents backward movement... - Mechanism of EF-Ts-catalyzed guanine nucleotide exchange in EF-Tu: contribution of interactions mediated by helix B of EF-TuTobias Schümmer
Institute of Physical Biochemistry, University of Witten Herdecke, D 58448 Witten, Germany
Biochemistry 46:4977-84. 2007.... - Signal sequence-independent membrane targeting of ribosomes containing short nascent peptides within the exit tunnelThomas Bornemann
Institute of Molecular Biology, University of Witten Herdecke, Stockumer Strasse 10, 55448 Witten, Germany
Nat Struct Mol Biol 15:494-9. 2008.... - Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomesLorna E Lancaster
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
Mol Microbiol 69:390-401. 2008..The tRNA-mRNA translocation is faster on colicin E3-cleaved than on intact ribosomes and is less sensitive to inhibition by the antibiotic viomycin... - Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosomeVladimir I Katunin
Institutes of Molecular Biology and Physical Biochemistry, University of Witten/Herdecke, 58448 Witten, Germany
Biochemistry 41:12806-12. 2002.... - An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocationAndreas Savelsbergh
Institute of Molecular Biology, University of Witten/Herdecke, 58448 Witten, Germany
Mol Cell 11:1517-23. 2003..These results indicate that the energy of GTP hydrolysis is utilized to promote the ribosome rearrangement and to bias spontaneous fluctuations within the ribosome-EF-G complex toward unidirectional movement of mRNA and tRNA... - Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNAKirill B Gromadski
Institute of Physical Biochemistry, University of Witten Herdecke, Stockumer Strasse 10, D 58448 Witten, Germany
J Biol Chem 282:35629-37. 2007..eEF1A.GTP binds Phe-tRNA(Phe) with a K(d) of 3 nm, whereas eEF1A.GDP shows no significant binding, indicating that eEF1A has similar tRNA binding properties as its prokaryotic homolog, EF-Tu... - Distinct functions of elongation factor G in ribosome recycling and translocationAndreas Savelsbergh
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
RNA 15:772-80. 2009.... - Trigger factor binds to ribosome-signal-recognition particle (SRP) complexes and is excluded by binding of the SRP receptorIwona Buskiewicz
Institute für Molekularbiologie und Physikalische Biochemie, Universitat Witten Herdecke, 58448 Witten, Germany
Proc Natl Acad Sci U S A 101:7902-6. 2004.... - Kinetic mechanism of elongation factor Ts-catalyzed nucleotide exchange in elongation factor TuKirill B Gromadski
Institute of Physical Biochemistry, University of Witten Herdecke, D 58448 Witten, Germany
Biochemistry 41:162-9. 2002..At in vivo concentrations of nucleotides and factors, the overall exchange rate, as calculated from the elemental rate constants, is 30 s(-1), which is compatible with the rate of protein synthesis in the cell... - Involvement of helix 34 of 16 S rRNA in decoding and translocation on the ribosomeAndrew Kubarenko
Institute of Physical Biochemistry, University of Witten Herdecke, 58448 Witten, Germany
J Biol Chem 281:35235-44. 2006..The data indicate that helix 34 is involved in controlling the maintenance of the reading frame and in tRNA translocation... - Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRETIwona Buskiewicz
Institute of Molecular Biology, University of Witten Herdecke, 58448 Witten, Germany
J Mol Biol 351:417-30. 2005..The domain rearrangement of Ffh that takes place upon formation of the SRP is probably important for subsequent steps of membrane targeting, including interactions with the translating ribosome and the SRP receptor... - Single-step purification of specific tRNAs by hydrophobic taggingUte Kothe
Institute of Physical Biochemistry, University of Witten/Herdecke, D-58448 Witten, Germany
Anal Biochem 356:148-50. 2006 - Domain rearrangement of SRP protein Ffh upon binding 4.5S RNA and the SRP receptor FtsYIwona Buskiewicz
Institute of Molecular Biology, University of Witten Herdecke, Germany
RNA 11:947-57. 2005..These results suggest that in free Ffh, the binding sites for 4.5S RNA and FtsY are occluded by strong domain-domain interactions which must be disrupted for the formation of SRP or the Ffh-FtsY complex... - The ribosome-bound initiation factor 2 recruits initiator tRNA to the 30S initiation complexPohl Milon
Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, Göttingen 37077, Germany
EMBO Rep 11:312-6. 2010..The mechanism of action of IF2 seems to be different from that of tRNA carriers such as EF-Tu, SelB and eukaryotic initiation factor 2 (eIF2), instead resembling that of eIF5B, the eukaryotic subunit association factor... - Recent mechanistic insights into eukaryotic ribosomesMarina V Rodnina
Max Planck Institute for Biophysical Chemistry, Department of Physical Biochemistry, 37077 Gottingen, Germany
Curr Opin Cell Biol 21:435-43. 2009..Here, we summarize recent progress in deciphering molecular mechanisms of eukaryotic translation. Comparisons with prokaryotic translation are included, emphasizing emerging patterns of common design... - The ribosome goes NobelMarina V Rodnina
Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, 37077 Goettingen, Germany
Trends Biochem Sci 35:1-5. 2010..The award of this year's Nobel Prize in Chemistry to Ada E. Yonath, Venkatraman Ramakrishnan and Thomas A. Steitz honors their breakthrough achievement in determining the atomic structure of the ribosome... - Towards understanding selenocysteine incorporation into bacterial proteinsNiels Fischer
3D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, D 37077 Gottingen, Germany
Biol Chem 388:1061-7. 2007..The results indicate that mthSelA forms a homodecamer that has a ring-like structure with five bilobed wings, similar to the structure of the E. coli complex determined previously... - Purine bases at position 37 of tRNA stabilize codon-anticodon interaction in the ribosomal A site by stacking and Mg2+-dependent interactionsAndrey L Konevega
Petersburg Nuclear Physics Institute, Russian Academy of Sciences, 188300 Gatchina, Russia
RNA 10:90-101. 2004.... - Kinetic analysis of interaction of eukaryotic release factor 3 with guanine nucleotidesVera P Pisareva
Department of Microbiology and Immunology, State University of New York Downstate Medical Center, Brooklyn, New York 11203, USA
J Biol Chem 281:40224-35. 2006..Guanine nucleotide binding and exchange on eRF3, which therefore depends on stimulation by eRF1, is entirely different from that on prokaryotic RF3 and unusual among GTPases... - The ribosome as an entropy trapAnnette Sievers
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA
Proc Natl Acad Sci U S A 101:7897-901. 2004..These results are consistent with the view that the ribosome enhances the rate of peptide bond formation mainly by positioning the substrates and/or water exclusion within the active site, rather than by conventional chemical catalysis... - 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... - Structural and functional investigation of a putative archaeal selenocysteine synthaseJens T Kaiser
Division of Chemistry and Chemical Engineering, California Institute of Technology, M C 114 96, Pasadena, California 91125, USA
Biochemistry 44:13315-27. 2005.... - The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensorPohl Milon
Laboratory of Genetics, Department of Biology MCA, University of Camerino, 62032 Camerino MC, Italy
Proc Natl Acad Sci U S A 103:13962-7. 2006.... - Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosomeVladimir I Katunin
Sankt Petersburg Nuclear Physics Institute, Russian Academy of Sciences, Gatchina, Russia
Mol Cell 10:339-46. 2002..These results suggest a contribution to overall catalysis of general acid-base and/or conformational catalysis involving an ionizing group at the active site... - Exploration of the conserved A+C wobble pair within the ribosomal peptidyl transferase center using affinity purified mutant ribosomesAshley Eversole Hesslein
Yale University, Department of Molecular Biophysics and Biochemistry, 260 Whitney Avenue, New Haven, CT 06520 8114, USA
Nucleic Acids Res 32:3760-70. 2004.... - The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchangeLouise D Dahl
Department of Molecular Biology, Aarhus University, Denmark
J Biol Chem 281:21139-46. 2006..The mutations had no effect on EF-Tu-dependent delivery of aminoacyl-tRNA to the ribosome... - Kinetic checkpoint at a late step in translation initiationPohl Milon
Department of Biology MCA, Laboratory of Genetics, University of Camerino, 62032 Camerino, Italy
Mol Cell 30:712-20. 2008.... - Transient kinetics, fluorescence, and FRET in studies of initiation of translation in bacteriaPohl Milon
Laboratory of Genetics, Department of Biology MCA, University of Camerino, Camerino, Italy
Methods Enzymol 430:1-30. 2007..The methods described here are based on results obtained with initiation components from Escherichia coli but can be adopted for mechanistic studies of initiation in other prokaryotic or eukaryotic systems... - An uncharged amine in the transition state of the ribosomal peptidyl transfer reactionDavid A Kingery
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA
Chem Biol 15:493-500. 2008..Such a transition state is significantly different from that of uncatalyzed aminolysis reactions in solution... - Inactivation of the elongation factor Tu by mosquitocidal toxin-catalyzed mono-ADP-ribosylationJörg Schirmer
Institut fur Experimentelle und Klinische Pharmakologie und Toxikologie, Albert Ludwigs Universitat Freiburg, D 79104 Freiburg, Germany
Appl Environ Microbiol 68:4894-9. 2002..The inactivation of EF-Tu by MTX-mediated ADP-ribosylation and the resulting inhibition of bacterial protein synthesis are likely to play important roles in the cytotoxicity of the 27-kDa enzyme fragment of MTX toward E. coli...