Senyushkina, Tamara

[["dc.bibliographiccitation.artnumber","7442"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.lastpage","11"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Adio, Sarah"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Fischer, Niels"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:44:23Z"],["dc.date.available","2017-09-07T11:44:23Z"],["dc.date.issued","2015"],["dc.description.abstract","The coupled translocation of transfer RNA and messenger RNA through the ribosome entails large-scale structural rearrangements, including step-wise movements of the tRNAs. Recent structural work has visualized intermediates of translocation induced by elongation factor G (EF-G) with tRNAs trapped in chimeric states with respect to 30S and 50S ribosomal subunits. The functional role of the chimeric states is not known. Here we follow the formation of translocation intermediates by single-molecule fluorescence resonance energy transfer. Using EF-G mutants, a non-hydrolysable GTP analogue, and fusidic acid, we interfere with either translocation or EF-G release from the ribosome and identify several rapidly interconverting chimeric tRNA states on the reaction pathway. EF-G engagement prevents backward transitions early in translocation and increases the fraction of ribosomes that rapidly fluctuate between hybrid, chimeric and posttranslocation states. Thus, the engagement of EF-G alters the energetics of translocation towards a flat energy landscape, thereby promoting forward tRNA movement."],["dc.identifier.doi","10.1038/ncomms8442"],["dc.identifier.gro","3141892"],["dc.identifier.isi","000357176700008"],["dc.identifier.pmid","26072700"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2234"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2041-1723"],["dc.title","Fluctuations between multiple EF-G-induced chimeric tRNA states during 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","258a"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Adio, Sarah"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2022-03-01T11:44:56Z"],["dc.date.available","2022-03-01T11:44:56Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bpj.2012.11.1448"],["dc.identifier.pii","S000634951202694X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103166"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0006-3495"],["dc.title","Translocation of tRNAs through the Ribosome followed by Single Molecule FRET"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["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.issue","6"],["dc.bibliographiccitation.journal","Science Advances"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Klimova, M."],["dc.contributor.author","Senyushkina, T."],["dc.contributor.author","Samatova, E."],["dc.contributor.author","Peng, B. Z."],["dc.contributor.author","Pearson, M."],["dc.contributor.author","Peske, F."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:47:16Z"],["dc.date.available","2022-03-01T11:47:16Z"],["dc.date.issued","2019"],["dc.description.abstract","Translational translocase pushes hyper-rotated ribosomes to slide along the noncoding mRNA gap at the cost of GTP hydrolysis."],["dc.description.abstract","Translational bypassing is a recoding event during which ribosomes slide over a noncoding region of the messenger RNA (mRNA) to synthesize one protein from two discontinuous reading frames. Structures in the mRNA orchestrate forward movement of the ribosome, but what causes ribosomes to start sliding remains unclear. Here, we show that elongation factor G (EF-G) triggers ribosome take-off by a pseudotranslocation event using a small mRNA stem-loop as an A-site transfer RNA mimic and requires hydrolysis of about two molecules of guanosine 5′-triphosphate per nucleotide of the noncoding gap. Bypassing ribosomes adopt a hyper-rotated conformation, also observed with ribosomes stalled by the SecM sequence, suggesting common ribosome dynamics during translation stalling. Our results demonstrate a new function of EF-G in promoting ribosome sliding along the mRNA, in contrast to codon-wise ribosome movement during canonical translation, and suggest a mechanism by which ribosomes could traverse untranslated parts of mRNAs."],["dc.description.abstract","Translational translocase pushes hyper-rotated ribosomes to slide along the noncoding mRNA gap at the cost of GTP hydrolysis."],["dc.description.abstract","Translational bypassing is a recoding event during which ribosomes slide over a noncoding region of the messenger RNA (mRNA) to synthesize one protein from two discontinuous reading frames. Structures in the mRNA orchestrate forward movement of the ribosome, but what causes ribosomes to start sliding remains unclear. Here, we show that elongation factor G (EF-G) triggers ribosome take-off by a pseudotranslocation event using a small mRNA stem-loop as an A-site transfer RNA mimic and requires hydrolysis of about two molecules of guanosine 5′-triphosphate per nucleotide of the noncoding gap. Bypassing ribosomes adopt a hyper-rotated conformation, also observed with ribosomes stalled by the SecM sequence, suggesting common ribosome dynamics during translation stalling. Our results demonstrate a new function of EF-G in promoting ribosome sliding along the mRNA, in contrast to codon-wise ribosome movement during canonical translation, and suggest a mechanism by which ribosomes could traverse untranslated parts of mRNAs."],["dc.identifier.doi","10.1126/sciadv.aaw9049"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103975"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2375-2548"],["dc.title","EF-G–induced ribosome sliding along the noncoding mRNA"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1332"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Nature structural & molecular biology"],["dc.bibliographiccitation.lastpage","1337"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Lee, Sejeong"],["dc.contributor.author","Bornemann, Thomas"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2018-01-29T11:01:49Z"],["dc.date.available","2018-01-29T11:01:49Z"],["dc.date.issued","2012"],["dc.description.abstract","Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show that after initial binding to the ribosome, SRP undergoes dynamic fluctuations in search of additional interactions. Non-translating ribosomes, or ribosomes synthesizing non-membrane proteins, do not provide these contacts, allowing SRPs to dissociate rapidly. A nascent peptide in the exit tunnel stabilizes SRPs in a standby state. Binding to the emerging signal-anchor sequence (SAS) of a nascent membrane protein halts the fluctuations of SRP, resulting in complex stabilization and recruitment of the SRP receptor. We propose a kinetic model where SRP rapidly scans all ribosomes until it encounters a ribosome exposing an SAS. Binding to the SAS switches SRP into the targeting mode, in which dissociation is slow and docking of the SRP receptor is accelerated."],["dc.identifier.doi","10.1038/nsmb.2421"],["dc.identifier.pmid","23142984"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11868"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1545-9985"],["dc.title","Dynamic switch of the signal recognition particle from scanning to targeting"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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"]]

[["dc.bibliographiccitation.firstpage","2187"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","2196"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Sharma, Heena"],["dc.contributor.author","Adio, Sarah"],["dc.contributor.author","Senyushkina, Tamara"],["dc.contributor.author","Belardinelli, Riccardo"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:44:43Z"],["dc.date.available","2017-09-07T11:44:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Ribosome dynamics play an important role in translation. The rotation of the ribosomal subunits relative to one another is essential for tRNA-mRNA translocation. An important unresolved question is whether subunit rotation limits the rate of translocation. Here, we monitor subunit rotation relative to peptide bond formation and translocation using ensemble kinetics and single-molecule FRET. We observe that spontaneous forward subunit rotation occurs at a rate of 40 s(-1), independent of the rate of preceding peptide bond formation. Elongation factor G (EF-G) accelerates forward subunit rotation to 200 s(-1). tRNA-mRNA movement is much slower (10-40 s(-1)), suggesting that forward subunit rotation does not limit the rate of translocation. The transition back to the non-rotated state of the ribosome kinetically coincides with tRNA-mRNA movement. Thus, largescale movements of the ribosome are intrinsically rapid and gated by its ligands such as EF-G and tRNA."],["dc.identifier.doi","10.1016/j.celrep.2016.07.051"],["dc.identifier.gro","3141633"],["dc.identifier.isi","000382310100015"],["dc.identifier.pmid","27524615"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3456"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Deutsche Forschungsgemeinschaft [Sonderforschungsbereich 860]"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","2211-1247"],["dc.title","Kinetics of Spontaneous and EF-G-Accelerated Rotation of Ribosomal Subunits"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]