Rodnina, Marina V.

[["dc.bibliographiccitation.firstpage","390"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","401"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Lancaster, Lorna E."],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Kleanthous, Colin"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T15:14:13Z"],["dc.date.available","2018-01-29T15:14:13Z"],["dc.date.issued","2008"],["dc.description.abstract","The cytotoxin colicin E3 targets the 30S subunit of bacterial ribosomes and specifically cleaves 16S rRNA at the decoding centre, thereby inhibiting translation. Although the cleavage site is well known, it is not clear which step of translation is inhibited. We studied the effects of colicin E3 cleavage on ribosome functions by analysing individual steps of protein synthesis. We find that the cleavage affects predominantly the elongation step. The inhibitory effect of colicin E3 cleavage originates from the accumulation of sequential impaired decoding events, each of which results in low occupancy of the A site and, consequently, decreasing yield of elongating peptide. The accumulation leads to an almost complete halt of translation after reading of a few codons. The cleavage of 16S rRNA does not impair monitoring of codon-anticodon complexes or GTPase activation during elongation-factor Tu-dependent binding of aminoacyl-tRNA, but decreases the stability of the codon-recognition complex and slows down aminoacyl-tRNA accommodation in the A site. The tRNA-mRNA translocation is faster on colicin E3-cleaved than on intact ribosomes and is less sensitive to inhibition by the antibiotic viomycin."],["dc.identifier.doi","10.1111/j.1365-2958.2008.06283.x"],["dc.identifier.pmid","18485067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11894"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1365-2958"],["dc.title","Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1183"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","1194"],["dc.bibliographiccitation.volume","343"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Katunin, Vladimir I."],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:43:10Z"],["dc.date.available","2017-09-07T11:43:10Z"],["dc.date.issued","2004"],["dc.description.abstract","Translocation, a coordinated movement of two tRNAs together with mRNA on the ribosome, is catalyzed by elongation factor G (EF-G). The reaction is accompanied by conformational rearrangements of the ribosome that are, as yet, not well characterized. Here, we analyze those rearrangements by restricting the conformational flexibility of the ribosome by antibiotics binding to specific sites of the ribosome. Paromomycin (Par), viomycin (Vio), spectinomycin (Spc), and hygromycin B (HygB) inhibited the tRNA-mRNA movement, while the other partial reactions of translocation, including the unlocking rearrangement of the ribosome that precedes tRNA-mRNA movement, were not affected. The functional cycle of EF-G, i.e. binding of EF-G(.)GTP to the ribosome, GTP hydrolysis, Pi release, and dissociation of EF-G(.)GDP from the ribosome, was not affected either, indicating that EF-G turnover is not coupled directly to tRNA-mRNA movement. The inhibition of translocation. by Par and Vio is attributed to the stabilization of tRNA binding in the A site, whereas Spc and HygB had a direct inhibitory effect on tRNA-mRNA movement. Streptomycin (Str) had essentially no effect on translocation, although it caused a large increase in tRNA affinity to the A site. These results suggest that conformational changes in the vicinity of the decoding region at the binding sites of Spc and HygB are important for tRNA-mRNA movement, whereas Str seems to stabilize a conformation of the ribosome that is prone to rapid translocation, thereby compensating the effect on tRNA affinity. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2004.08.097"],["dc.identifier.gro","3143929"],["dc.identifier.isi","000224838800003"],["dc.identifier.pmid","15491605"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1497"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","301"],["dc.bibliographiccitation.lastpage","318"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Matassova, Natalia B."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Pape, Tillmann"],["dc.contributor.author","Mohr, Dagmar"],["dc.contributor.editor","Garrett, Roger A."],["dc.date.accessioned","2017-09-07T11:54:06Z"],["dc.date.available","2017-09-07T11:54:06Z"],["dc.date.issued","2014"],["dc.description.abstract","This chapter concentrates on pre-steady-state kinetic work, and provides evidence on how much the interpretation of kinetic results in molecular-mechanistic terms owes to structural information obtained from crystallography and cryo-electron microscopy. Our studies of elongation factor (EF-Tu) function address two main issues: (i) the elucidation of the reaction pathway to identify intermediate steps of A-site binding and (ii) the quantitative evaluation of the pathway in order to understand specificity. Based on measured rates of GTP hydrolysis and peptide bond formation, Thompson and colleagues proposed that the rate of GTP hydrolysis by EF-Tu is independent of the tRNA, thereby providing an internal kinetic standard for translational accuracy. Binding of thiostrepton to the 1070 region of 23S rRNA interferes with translocation, as it strongly inhibits Pi release, translocation, and subsequent turnover of EF-G; in contrast, EF-G binding and GTP hydrolysis are not affected. The GTPase activities of EF-Tu and EF-G intrinsically are very low and are strongly enhanced on the ribosome. Recently, the ability of isolated L12 protein to stimulate GTP hydrolysis by either EF-Tu or EF-G, has been studied. In the fusidic acid-stabilized complex of EF-G with the ribosome, the α- sarcin stem is close to position 196 in the G domain of EF-G, which lies just above the GTP binding site, while the α-sarcin loop region is in the vicinity of position 650 in domain 5 of the factor."],["dc.identifier.doi","10.1128/9781555818142.ch25"],["dc.identifier.gro","3145105"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2805"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.publisher","American Society for Microbiology Press"],["dc.publisher.place","Washington, DC"],["dc.relation.doi","10.1128/9781555818142"],["dc.relation.isbn","1-55581-184-1"],["dc.relation.isbn","978-1-55581-184-6"],["dc.relation.ispartof","The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions"],["dc.title","Mechanisms of Partial Reactions of the Elongation Cycle Catalyzed by Elongation Factors Tu and G"],["dc.type","book_chapter"],["dc.type.internalPublication","no"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","559"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Biology"],["dc.bibliographiccitation.lastpage","568"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Semenkov, Yuri P."],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Katunin, Vladimir I."],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Wilden, Berthold"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:46:05Z"],["dc.date.available","2017-09-07T11:46:05Z"],["dc.date.issued","2001"],["dc.description.abstract","During the translocation step of the elongation cycle of peptide synthesis two tRNAs together with the mRNA move synchronously and rapidly on the ribosome. Translocation is catalyzed by the elongation factor G (EF-G) and requires GTP hydrolysis. The fundamental biochemical features of the process were worked out in the 1970-80s, to a large part by A.S. Spirin and his colleagues. Recent results from pre-steady-state kinetic analysis and cryoelectron microscopy suggest that translocation is a multistep dynamic process that entails large-scale structural rearrangements of both ribosome and EF-G. Kinetic and thermodynamic data, together with the structural information on the conformational changes in the ribosome and EF-G, provide a detailed mechanistic model of translocation and suggest a mechanism of translocation catalysis by EF-G."],["dc.identifier.doi","10.1023/A:1010523026531"],["dc.identifier.gro","3144276"],["dc.identifier.isi","000170715300012"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1882"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Consultants Bureau"],["dc.relation.issn","0026-8933"],["dc.title","Mechanism of tRNA translocation on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4316"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","4323"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Mohr, Dagmar"],["dc.contributor.author","Kothe, Ute"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:53:35Z"],["dc.date.available","2017-09-07T11:53:35Z"],["dc.date.issued","2005"],["dc.description.abstract","Ribosomal protein L7/12 is crucial for the function of elongation factor G (EF-G) on the ribosome. Here, we report the localization of a site in the C-terminal domain (CTD) of L7/12 that is critical for the interaction with EF-G. Single conserved surface amino acids were replaced in the CTD of L7/12. Whereas mutations in helices 5 and 6 had no effect, replacements of V66,169, K70, and R73 in helix 4 increased the Michaelis constant (K-M) of EF-G.GTP for the ribosome, suggesting an involvement of these residues in EF-G binding. The mutations did not appreciably affect rapid single-round GTP hydrolysis and had no effect on tRNA translocation on the ribosome. in contrast, the release of inorganic phosphate (Pi) from ribosome-bound EF-G.GDP.Pi was strongly inhibited and became rate-limiting for the turnover of EF-G. The control of Pi release by interactions between EF-G and L7/12 appears to be important for maintaining the conformational coupling between EF-G and the ribosome for translocation and for timing the dissociation of the factor from the ribosome."],["dc.identifier.doi","10.1038/sj.emboj.7600884"],["dc.identifier.gro","3143769"],["dc.identifier.isi","000234805100010"],["dc.identifier.pmid","16292341"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1319"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.title","Control of phosphate release from elongation factor G by ribosomal protein L7/12"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12806"],["dc.bibliographiccitation.issue","42"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","12812"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Katunin, Vladimir I."],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:45:13Z"],["dc.date.available","2017-09-07T11:45:13Z"],["dc.date.issued","2002"],["dc.description.abstract","The translocation step of elongation entails the coordinated movement of tRNA and mRNA on the ribosome. Translocation is promoted by elongation factor G (EF-G) and accompanied by GTP hydrolysis, which affects both translocation and turnover of EF-G. Both reactions are much slower (50-100-fold) when GTP is replaced with non-hydrolyzable GTP analogues or GDP, indicating that the reaction rates are determined by conformational transitions induced by GTP hydrolysis. Compared to the rate of uncatalyzed, spontaneous translocation, ribosome binding of EF-G with any guanine nucleotide reduces the free energy of activation by about 18 kJ/mol, whereas GTP hydrolysis contributes another 10 kJ/mol. The acceleration by GTP hydrolysis is due to large decrease in activation enthalpy by about 30 kJ/mol, compared to the reaction with GTP analogues or GDP, whereas the activation entropy becomes unfavorable and is lowered by about 20 kJ/mol (37 degreesC). The data suggest that GTP hydrolysis induces, by a conformational change of EF-G, a rapid conformational rearrangement of the ribosome (\"unlocking\") which determines the rates of both tRNA-mRNA translocation and recycling of the factor."],["dc.identifier.doi","10.1021/bi0264871"],["dc.identifier.gro","3144161"],["dc.identifier.isi","000178694000026"],["dc.identifier.pmid","12379123"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1754"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","377"],["dc.bibliographiccitation.issue","5-6"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.lastpage","387"],["dc.bibliographiccitation.volume","381"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Stark, Holger"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Wieden, Hans-Joachim"],["dc.contributor.author","Mohr, Dagmar"],["dc.contributor.author","Matassova, Natalia B."],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Daviter, T"],["dc.contributor.author","Gualerzi, Claudio O."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:47:23Z"],["dc.date.available","2017-09-07T11:47:23Z"],["dc.date.issued","2000"],["dc.description.abstract","The elongation factors (EF) Tu and G and initiation factor 2 (IF2) from bacteria are multidomain GTPases with essential functions in the elongation and initiation phases of translation. They bind to the same site on the ribosome where their low intrinsic GTPase activities are strongly stimulated. The factors differ fundamentally from each other, and from the majority of GTPases, in the mechanisms of GTPase control, the timing of P-i release, and the functional role of GTP hydrolysis. EF-Tu GTP forms a ternary complex with aminoacyl-tRNA, which binds to the ribosome, Only when a matching codon is recognized, the GTPase of EF-Tu is stimulated, rapid GTP hydrolysis and P-i release take place, EF-Tu rearranges to the GDP form, and aminoacyl-tRNA is released into the peptidyltransferase center. In contrast, EF-G hydrolyzes GTP immediately upon binding to the ribosome, stimulated by ribosomal protein L7/12. Subsequent translocation is driven by the slow dissociation of P-i, suggesting a mechano-chemical function of EF-G, Accordingly, different conformations of EF-G on the ribosome are revealed by cryo-electron microscopy. GTP hydrolysis by IF2 is triggered upon formation of the 70S initiation complex, and the dissociation of P-i and/or IF2 follows a rearrangement of the ribosome into the elongation-competent state."],["dc.identifier.doi","10.1515/BC.2000.050"],["dc.identifier.gro","3144395"],["dc.identifier.isi","000088435900004"],["dc.identifier.pmid","10937868"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2015"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Walter De Gruyter & Co"],["dc.relation.issn","1431-6730"],["dc.title","GTPase mechanisms and functions of translation factors on the ribosome"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2102"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","2107"],["dc.bibliographiccitation.volume","109"],["dc.contributor.author","Cox, Georgina"],["dc.contributor.author","Thompson, Gary S."],["dc.contributor.author","Jenkins, Huw T."],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Homans, Steve W."],["dc.contributor.author","Edwards, Thomas A."],["dc.contributor.author","O'Neill, Alexander J."],["dc.date.accessioned","2018-01-29T12:41:47Z"],["dc.date.available","2018-01-29T12:41:47Z"],["dc.date.issued","2012"],["dc.description.abstract","Resistance to the antibiotic fusidic acid (FA) in the human pathogen Staphylococcus aureus usually results from expression of FusB-type proteins (FusB or FusC). These proteins bind to elongation factor G (EF-G), the target of FA, and rescue translation from FA-mediated inhibition by an unknown mechanism. Here we show that the FusB family are two-domain metalloproteins, the C-terminal domain of which contains a four-cysteine zinc finger with a unique structural fold. This domain mediates a high-affinity interaction with the C-terminal domains of EF-G. By binding to EF-G on the ribosome, FusB-type proteins promote the dissociation of stalled ribosome⋅EF-G⋅GDP complexes that form in the presence of FA, thereby allowing the ribosomes to resume translation. Ribosome clearance by these proteins represents a highly unusual antibiotic resistance mechanism, which appears to be fine-tuned by the relative abundance of FusB-type protein, ribosomes, and EF-G."],["dc.identifier.doi","10.1073/pnas.1117275109"],["dc.identifier.pmid","22308410"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11881"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1091-6490"],["dc.title","Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","37"],["dc.bibliographiccitation.issue","6611"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","41"],["dc.bibliographiccitation.volume","385"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Katunin, Vladimir I."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:51:01Z"],["dc.date.available","2017-09-07T11:51:01Z"],["dc.date.issued","1997"],["dc.description.abstract","Elongation factor G (EF-G) is a GTPase that is involved in the translocation of bacterial ribosomes along messenger RNA during protein biosynthesis. In contrast to current models, EF-G-dependent GTP hydrolysis is shown to precede, and greatly accelerate, the rearrangement of the ribosome that leads to translocation. Domain IV of the EF-G structure is crucial for both rapid translocation and subsequent release of the factor from the ribosome. 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."],["dc.identifier.doi","10.1038/385037a0"],["dc.identifier.gro","3144617"],["dc.identifier.isi","A1997WA73100040"],["dc.identifier.pmid","8985244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2261"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Macmillan Magazines Ltd"],["dc.relation.issn","0028-0836"],["dc.title","Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","772"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","780"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:47:30Z"],["dc.date.available","2017-09-07T11:47:30Z"],["dc.date.issued","2009"],["dc.description.abstract","Elongation factor G (EF-G) promotes the translocation step in bacterial protein synthesis and, together with ribosome recycling factor (RRF), the disassembly of the post-termination ribosome. Unlike translocation, ribosome disassembly strictly requires GTP hydrolysis by EF-G. Here we report that ribosome disassembly is strongly inhibited by vanadate, an analog of inorganic phosphate (Pi), indicating that Pi release is required for ribosome disassembly. In contrast, the function of EF-G in single-round translocation is not affected by vanadate, while the turnover reaction is strongly inhibited. We also show that the antibiotic fusidic acid blocks ribosome disassembly by EF-G/RRF at a 1000-fold lower concentration than required for the inhibition of EF-G turnover in vitro and close to the effective inhibitory concentration in vivo, suggesting that the antimicrobial activity of fusidic acid is primarily due to the direct inhibition of ribosome recycling. Our results indicate that conformational coupling between EF-G and the ribosome is principally different in translocation and ribosome disassembly. Pi release is not required for the mechanochemical function of EF-G in translocation, whereas the interactions between RRF and EF-G introduce tight coupling between the conformational change of EF-G induced by Pi release and ribosome disassembly."],["dc.identifier.doi","10.1261/rna.1592509"],["dc.identifier.gro","3143123"],["dc.identifier.isi","000265231500004"],["dc.identifier.pmid","19324963"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/603"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1355-8382"],["dc.title","Distinct functions of elongation factor G in ribosome recycling and translocation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]