Maracci, Cristina

[["dc.bibliographiccitation.firstpage","1056"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","1067"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Korniy, Natalia"],["dc.contributor.author","Klimova, Mariia"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Peng, Bee-Zen"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Belardinelli, Riccardo"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Peske, Frank"],["dc.date.accessioned","2022-03-01T11:46:50Z"],["dc.date.available","2022-03-01T11:46:50Z"],["dc.date.issued","2019"],["dc.description.abstract","Abstract During canonical translation, the ribosome moves along an mRNA from the start to the stop codon in exact steps of one codon at a time. The collinearity of the mRNA and the protein sequence is essential for the quality of the cellular proteome. Spontaneous errors in decoding or translocation are rare and result in a deficient protein. However, dedicated recoding signals in the mRNA can reprogram the ribosome to read the message in alternative ways. This review summarizes the recent advances in understanding the mechanisms of three types of recoding events: stop-codon readthrough, –1 ribosome frameshifting and translational bypassing. Recoding events provide insights into alternative modes of ribosome dynamics that are potentially applicable to other non-canonical modes of prokaryotic and eukaryotic translation."],["dc.description.abstract","Abstract During canonical translation, the ribosome moves along an mRNA from the start to the stop codon in exact steps of one codon at a time. The collinearity of the mRNA and the protein sequence is essential for the quality of the cellular proteome. Spontaneous errors in decoding or translocation are rare and result in a deficient protein. However, dedicated recoding signals in the mRNA can reprogram the ribosome to read the message in alternative ways. This review summarizes the recent advances in understanding the mechanisms of three types of recoding events: stop-codon readthrough, –1 ribosome frameshifting and translational bypassing. Recoding events provide insights into alternative modes of ribosome dynamics that are potentially applicable to other non-canonical modes of prokaryotic and eukaryotic translation."],["dc.identifier.doi","10.1093/nar/gkz783"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103816"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","Translational recoding: canonical translation mechanisms reinterpreted"],["dc.type","journal_article"],["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.journal","eLife"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Adio, Sarah"],["dc.contributor.author","Sharma, Heena"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Maracci, Cristina"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2019-07-25T11:30:31Z"],["dc.date.available","2019-07-25T11:30:31Z"],["dc.date.issued","2018"],["dc.description.abstract","Release factors RF1 and RF2 promote hydrolysis of peptidyl-tRNA during translation termination. The GTPase RF3 promotes recycling of RF1 and RF2. Using single molecule FRET and biochemical assays, we show that ribosome termination complexes that carry two factors, RF1-RF3 or RF2-RF3, are dynamic and fluctuate between non-rotated and rotated states, whereas each factor alone has its distinct signature on ribosome dynamics and conformation. Dissociation of RF1 depends on peptide release and the presence of RF3, whereas RF2 can dissociate spontaneously. RF3 binds in the GTP-bound state and can rapidly dissociate without GTP hydrolysis from termination complex carrying RF1. In the absence of RF1, RF3 is stalled on ribosomes if GTP hydrolysis is blocked. Our data suggest how the assembly of the ribosome-RF1-RF3-GTP complex, peptide release, and ribosome fluctuations promote termination of protein synthesis and recycling of the release factors."],["dc.identifier.doi","10.7554/eLife.34252"],["dc.identifier.pmid","29889659"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62052"],["dc.language.iso","en"],["dc.relation.eissn","2050-084X"],["dc.relation.issn","2050-084X"],["dc.title","Dynamics of ribosomes and release factors during translation termination in E. coli"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]