Pohl, Corinna

[["dc.bibliographiccitation.firstpage","3701"],["dc.bibliographiccitation.issue","21"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","3709"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:45:13Z"],["dc.date.available","2017-09-07T11:45:13Z"],["dc.date.issued","2010"],["dc.description.abstract","The speed and accuracy of protein synthesis are fundamental parameters for understanding the fitness of living cells, the quality control of translation, and the evolution of ribosomes. In this study, we analyse the speed and accuracy of the decoding step under conditions reproducing the high speed of translation in vivo. We show that error frequency is close to 10(-3), consistent with the values measured in vivo. Selectivity is predominantly due to the differences in k(cat) values for cognate and near-cognate reactions, whereas the intrinsic affinity differences are not used for tRNA discrimination. Thus, the ribosome seems to be optimized towards high speed of translation at the cost of fidelity. Competition with near-and non-cognate ternary complexes reduces the rate of GTP hydrolysis in the cognate ternary complex, but does not appreciably affect the rate-limiting tRNA accommodation step. 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. The EMBO Journal (2010) 29, 3701-3709. doi:10.1038/emboj.2010.229; Published online 14 September 2010"],["dc.identifier.doi","10.1038/emboj.2010.229"],["dc.identifier.gro","3142832"],["dc.identifier.isi","000285386700010"],["dc.identifier.pmid","20842102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/279"],["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","0261-4189"],["dc.title","Optimization of speed and accuracy of decoding in translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2979"],["dc.bibliographiccitation.journal","Philosophical Transactions of the Royal Society B: Biological Sciences"],["dc.bibliographiccitation.lastpage","2986"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Mittelstaet, Joerg"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T13:36:26Z"],["dc.date.available","2018-01-29T13:36:26Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1098/rstb.2011.0138"],["dc.identifier.eissn","1471-2970"],["dc.identifier.pmid","21930591"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11885"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.title","Evolutionary optimization of speed and accuracy of decoding on the ribosome"],["dc.type","review"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14418"],["dc.bibliographiccitation.issue","40"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","14423"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Dannies, Ev"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:45:27Z"],["dc.date.available","2017-09-07T11:45:27Z"],["dc.date.issued","2014"],["dc.description.abstract","GTP hydrolysis by elongation factor Tu (EF-Tu), a translational GTPase that delivers aminoacyl-tRNAs to the ribosome, plays a crucial role in decoding and translational fidelity. The basic reaction mechanism and the way the ribosome contributes to catalysis are a matter of debate. Here we use mutational analysis in combination with measurements of rate/pH profiles, kinetic solvent isotope effects, and ion dependence of GTP hydrolysis by EF-Tu off and on the ribosome to dissect the reaction mechanism. Our data suggest that-contrary to current models-the reaction in free EF-Tu follows a pathway that does not involve the critical residue H84 in the switch II region. Binding to the ribosome without a cognate codon in the A site has little effect on the GTPase mechanism. In contrast, upon cognate codon recognition, the ribosome induces a rearrangement of EF-Tu that renders GTP hydrolysis sensitive to mutations of Asp21 and His84 and insensitive to K+ ions. We suggest that Asp21 and His84 provide a network of interactions that stabilize the positions of the gamma-phosphate and the nucleophilic water, respectively, and thus play an indirect catalytic role in the GTPase mechanism on the ribosome."],["dc.identifier.doi","10.1073/pnas.1412676111"],["dc.identifier.gro","3142034"],["dc.identifier.isi","000342633900039"],["dc.identifier.pmid","25246550"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3812"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [FOR 1805]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0027-8424"],["dc.title","Ribosome-induced tuning of GTP hydrolysis by a translational GTPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e29525"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Tzivelekidis, Tina"],["dc.contributor.author","Jank, Thomas"],["dc.contributor.author","Pohl, Corinna"],["dc.contributor.author","Schlosser, Andreas"],["dc.contributor.author","Rospert, Sabine"],["dc.contributor.author","Knudsen, Charlotte R."],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Belyi, Yury"],["dc.contributor.author","Aktories, Klaus"],["dc.contributor.editor","Kwaik, Yousef Abu"],["dc.date.accessioned","2018-01-29T13:06:01Z"],["dc.date.available","2018-01-29T13:06:01Z"],["dc.date.issued","2011"],["dc.description.abstract","Legionella pneumophila, which is the causative organism of Legionnaireś disease, translocates numerous effector proteins into the host cell cytosol by a type IV secretion system during infection. Among the most potent effector proteins of Legionella are glucosyltransferases (lgt's), which selectively modify eukaryotic elongation factor (eEF) 1A at Ser-53 in the GTP binding domain. Glucosylation results in inhibition of protein synthesis. Here we show that in vitro glucosylation of yeast and mouse eEF1A by Lgt3 in the presence of the factors Phe-tRNA(Phe) and GTP was enhanced 150 and 590-fold, respectively. The glucosylation of eEF1A catalyzed by Lgt1 and 2 was increased about 70-fold. By comparison of uncharged tRNA with two distinct aminoacyl-tRNAs (His-tRNA(His) and Phe-tRNA(Phe)) we could show that aminoacylation is crucial for Lgt-catalyzed glucosylation. Aminoacyl-tRNA had no effect on the enzymatic properties of lgt's and did not enhance the glucosylation rate of eEF1A truncation mutants, consisting of the GTPase domain only or of a 5 kDa peptide covering Ser-53 of eEF1A. Furthermore, binding of aminoacyl-tRNA to eEF1A was not altered by glucosylation. Taken together, our data suggest that the ternary complex, consisting of eEF1A, aminoacyl-tRNA and GTP, is the bona fide substrate for lgt's."],["dc.identifier.doi","10.1371/journal.pone.0029525"],["dc.identifier.pmid","22216304"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11884"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1932-6203"],["dc.title","Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]