Rodnina, Marina V.

[["dc.bibliographiccitation.firstpage","1221"],["dc.bibliographiccitation.issue","11-12"],["dc.bibliographiccitation.journal","Biochemistry and Cell Biology"],["dc.bibliographiccitation.lastpage","1227"],["dc.bibliographiccitation.volume","73"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Fricke, Rainer"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Pape, Tillmann"],["dc.date.accessioned","2018-04-23T11:48:55Z"],["dc.date.available","2018-04-23T11:48:55Z"],["dc.date.issued","1995"],["dc.description.abstract","The mechanism of elongation factor Tu (EF-Tu) catalyzed aminoacyl-tRNA (aa-tRNA) binding to the A site of the ribosome was studied. Two types of complexes of EF-Tu with GTP and aa-tRNA, EF-Tu . GTP . aa-tRNA (ternary) and (EF-Tu . GTP)(2) . aa-tRNA (quinternary), can be formed in vitro depending on the conditions. On interaction with the ribosomal A site, generally only one molecule of GTP is hydrolysed per aa-tRNA bound and peptide bond formed. The second GTP molecule from the quinternary complex is hydrolyzed only during translation of an oligo(U) tract in the presence of EF-G. The first step in the interaction between the ribosome and the ternary complex is the codon-independent formation of an initial complex. In the absence of codon recognition, the aa-tRNA-EF-Tu complex does not enter further steps of A site binding and remains in the initial binding state. Despite the rapid formation of the initial complex, the rate constant of GTP hydrolysis in the noncognate complex is four orders of magnitude lower compared with the cognate complex. This, together with the results of time-resolved fluorescence measurements, suggests that codon recognition by the ternary complex on the ribosome initiates a series of structural rearrangements that result in a conformational change of EF-Tu, presumably involving the effector region, which, in turn, triggers GTP hydrolysis and the subsequent steps of A site binding."],["dc.identifier.doi","10.1139/o95-132"],["dc.identifier.gro","3144671"],["dc.identifier.isi","A1995UE60300052"],["dc.identifier.pmid","8722040"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2320"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0829-8211"],["dc.title","Elongation factor Tu, a GTPase triggered by codon recognition on the ribosome: mechanism and GTP consumption"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","317"],["dc.bibliographiccitation.lastpage","326"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Fricke, Rainer"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.editor","Nierhaus, Knud H."],["dc.contributor.editor","Franceschi, François"],["dc.contributor.editor","Subramanian, Alap R."],["dc.contributor.editor","Erdmann, Volker A."],["dc.contributor.editor","Wittmann-Liebold, Brigitte"],["dc.date.accessioned","2017-09-07T11:54:06Z"],["dc.date.available","2017-09-07T11:54:06Z"],["dc.date.issued","1993"],["dc.description.abstract","The elongation cycle of ribosomal protein synthesis begins with the binding of the substrate, aminoacyl-tRNA, to the A site of the ribosome. The reaction is a quite complex process which involves an enzyme, elongation factor Tu (EF-Tu), and GTP. It is the complex of aminoacyl-tRNA with EF-Tu and GTP (“ternary complex”) which rapidly associates with the A site (Miller and Weissbach, 1977; Kaziro, 1978). Subsequently, the recognition of the codon takes place. The formation of the codonanticodon complex provides the signal which triggers the hydrolysis of GTP. The latter enables the dissociation of EF-Tu•GDP from the ribosome which in turn allows the aminoacyl-tRNA to accommodate in the A site such as to be positioned correctly for peptidyl transfer. There is good evidence supporting the view that the complexity of the A-site binding reaction, at least in part, is due to the necessity to optimize speed and accuracy of aminoacyl-tRNA selection by the inclusion of proofreading during the process (Thompson and Dix, 1982; Thompson and Karim, 1982; Ehrenberg and Kurland, 1984; Ruusala et al., 1984)."],["dc.identifier.doi","10.1007/978-1-4615-2407-6_30"],["dc.identifier.gro","3145106"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2806"],["dc.language.iso","en"],["dc.notes","Printausgabe: Plenum Press, New York"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.publisher","Springer"],["dc.publisher.place","Boston"],["dc.relation.conference","International Conference on the Translational Apparatus"],["dc.relation.eventend","1992-11-05"],["dc.relation.eventlocation","Berlin"],["dc.relation.eventstart","1992-10-31"],["dc.relation.isbn","978-1-4613-6021-6"],["dc.relation.ispartof","The Translational Apparatus. Structure, Function, Regulation, Evolution"],["dc.title","Kinetic Fluorescence Study on EF-Tu-Dependent Binding of Phe-tRNAPhe to the Ribosomal a Site"],["dc.type","conference_paper"],["dc.type.internalPublication","no"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","646"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","652"],["dc.bibliographiccitation.volume","271"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Pape, Tillmann"],["dc.contributor.author","Fricke, Rainer"],["dc.contributor.author","Kuhn, Lothar"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2018-04-23T11:48:55Z"],["dc.date.available","2018-04-23T11:48:55Z"],["dc.date.issued","1996"],["dc.description.abstract","The first step in the sequence of interactions between the ribosome and the complex of elongation factor Tu (EF-Tu), GTP, and aminoacyl-tRNA, which eventually leads to A site-bound aminoacyl-tRNA, is the codon-independent formation of an initial complex. We have characterized the initial binding and the resulting complex by time-resolved (stopped-flow) and steady-state fluorescence measurements using several fluorescent tRNA derivatives. The complex is labile, with rate constants of 6 × 107M−1 s−1 and 24 s−1 (20°C, 10 mM Mg2+) for binding and dissociation, respectively. Both thermodynamic and activation parameters of initial binding were determined, and five Mg2+ ions were estimated to participate in the interaction. While a cognate ternary complex proceeds from initial binding through codon recognition to rapid GTP hydrolysis, the rate constant of GTP hydrolysis in the non-cognate complex is 4 orders of magnitude lower, despite the rapid formation of the initial complex in both cases. Hence, the ribosome-induced GTP hydrolysis by EF-Tu is strongly affected by the presence of the tRNA. This suggests that codon-anticodon recognition, which takes place after the formation of the initial binding complex, provides a specific signal that triggers fast GTP hydrolysis by EF-Tu on the ribosome."],["dc.identifier.doi","10.1074/jbc.271.2.646"],["dc.identifier.gro","3142457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13605"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0021-9258"],["dc.title","Initial Binding of the Elongation Factor Tu·GTP·Aminoacyl-tRNA Complex Preceding Codon Recognition on the Ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]