Samatova, Ekaterina N.

[["dc.bibliographiccitation.firstpage","5210"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","5222"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Korniy, Natalia"],["dc.contributor.author","Goyal, Akanksha"],["dc.contributor.author","Hoffmann, Markus"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Pöhlmann, Stefan"],["dc.contributor.author","Rodnina, Marina V"],["dc.date.accessioned","2020-12-10T18:19:35Z"],["dc.date.available","2020-12-10T18:19:35Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1093/nar/gkz202"],["dc.identifier.eissn","1362-4962"],["dc.identifier.issn","0305-1048"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16451"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75304"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","Modulation of HIV-1 Gag/Gag-Pol frameshifting by tRNA abundance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Daberger, Jan"],["dc.contributor.author","Liutkute, Marija"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:44:23Z"],["dc.date.available","2022-03-01T11:44:23Z"],["dc.date.issued","2021"],["dc.description.abstract","Protein homeostasis of bacterial cells is maintained by coordinated processes of protein production, folding, and degradation. Translational efficiency of a given mRNA depends on how often the ribosomes initiate synthesis of a new polypeptide and how quickly they read the coding sequence to produce a full-length protein. The pace of ribosomes along the mRNA is not uniform: periods of rapid synthesis are separated by pauses. Here, we summarize recent evidence on how ribosome pausing affects translational efficiency and protein folding. We discuss the factors that slow down translation elongation and affect the quality of the newly synthesized protein. Ribosome pausing emerges as important factor contributing to the regulatory programs that ensure the quality of the proteome and integrate the cellular and environmental cues into regulatory circuits of the cell."],["dc.description.abstract","Protein homeostasis of bacterial cells is maintained by coordinated processes of protein production, folding, and degradation. Translational efficiency of a given mRNA depends on how often the ribosomes initiate synthesis of a new polypeptide and how quickly they read the coding sequence to produce a full-length protein. The pace of ribosomes along the mRNA is not uniform: periods of rapid synthesis are separated by pauses. Here, we summarize recent evidence on how ribosome pausing affects translational efficiency and protein folding. We discuss the factors that slow down translation elongation and affect the quality of the newly synthesized protein. Ribosome pausing emerges as important factor contributing to the regulatory programs that ensure the quality of the proteome and integrate the cellular and environmental cues into regulatory circuits of the cell."],["dc.identifier.doi","10.3389/fmicb.2020.619430"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103010"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1664-302X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Translational Control by Ribosome Pausing in Bacteria: How a Non-uniform Pace of Translation Affects Protein Production and Folding"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Liutkute, Marija"],["dc.contributor.author","Maiti, Manisankar"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2021-03-05T08:59:20Z"],["dc.date.available","2021-03-05T08:59:20Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.7554/eLife.60895"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/80427"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-393"],["dc.relation.eissn","2050-084X"],["dc.title","Gradual compaction of the nascent peptide during cotranslational folding on the ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","189a"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biophysical Journal"],["dc.bibliographiccitation.lastpage","190a"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Liutkute, Marija"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Maiti, Manisankar"],["dc.contributor.author","Holtkamp, Wolf H."],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2020-12-10T14:22:45Z"],["dc.date.available","2020-12-10T14:22:45Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.bpj.2018.11.1050"],["dc.identifier.issn","0006-3495"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71722"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Monitoring Dynamics of Protein Nascent Chain on the Ribosome using PET-FCS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1468"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","1482"],["dc.bibliographiccitation.volume","593"],["dc.contributor.author","Korniy, Natalia"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Anokhina, Maria M."],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:44:42Z"],["dc.date.available","2022-03-01T11:44:42Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1002/1873-3468.13478"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103095"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1873-3468"],["dc.relation.issn","0014-5793"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc/4.0/"],["dc.title","Mechanisms and biomedical implications of –1 programmed ribosome frameshifting on viral and bacterial mRNAs"],["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.artnumber","4459"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.lastpage","10"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Konevega, Andrey L."],["dc.contributor.author","Wills, Norma M."],["dc.contributor.author","Atkins, John F."],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2017-09-07T11:46:11Z"],["dc.date.available","2017-09-07T11:46:11Z"],["dc.date.issued","2014"],["dc.description.abstract","The gene product 60 (gp60) of bacteriophage T4 is synthesized as a single polypeptide chain from a discontinuous reading frame as a result of bypassing of a non-coding mRNA region of 50 nucleotides by the ribosome. To identify the minimum set of signals required for bypassing, we recapitulated efficient translational bypassing in an in vitro reconstituted translation system from Escherichia coli. We find that the signals, which promote efficient and accurate bypassing, are specified by the gene 60 mRNA sequence. Systematic analysis of the mRNA suggests unexpected contributions of sequences upstream and downstream of the non-coding gap region as well as of the nascent peptide. During bypassing, ribosomes glide forward on the mRNA track in a processive way. Gliding may have a role not only for gp60 synthesis, but also during regular mRNA translation for reading frame selection during initiation or tRNA translocation during elongation."],["dc.identifier.doi","10.1038/ncomms5459"],["dc.identifier.gro","3142094"],["dc.identifier.isi","000340623400004"],["dc.identifier.pmid","25041899"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4478"],["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","High-efficiency translational bypassing of non-coding nucleotides specified by mRNA structure and nascent peptide"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Wohlgemuth, Ingo"],["dc.contributor.author","Garofalo, Raffaella"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Günenç, Aybeg Nafiz"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2021-06-01T10:50:39Z"],["dc.date.available","2021-06-01T10:50:39Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Aminoglycoside antibiotics target the ribosome and induce mistranslation, yet which translation errors induce bacterial cell death is unclear. The analysis of cellular proteins by quantitative mass spectrometry shows that bactericidal aminoglycosides induce not only single translation errors, but also clusters of errors in full-length proteins in vivo with as many as four amino acid substitutions in a row. The downstream errors in a cluster are up to 10,000-fold more frequent than the first error and independent of the intracellular aminoglycoside concentration. The prevalence, length, and composition of error clusters depends not only on the misreading propensity of a given aminoglycoside, but also on its ability to inhibit ribosome translocation along the mRNA. Error clusters constitute a distinct class of misreading events in vivo that may provide the predominant source of proteotoxic stress at low aminoglycoside concentration, which is particularly important for the autocatalytic uptake of the drugs."],["dc.identifier.doi","10.1038/s41467-021-21942-6"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/86738"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","2041-1723"],["dc.title","Translation error clusters induced by aminoglycoside antibiotics"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4369"],["dc.bibliographiccitation.issue","16"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","4387"],["dc.bibliographiccitation.volume","432"],["dc.contributor.author","O'Loughlin, Sinéad"],["dc.contributor.author","Capece, Mark C."],["dc.contributor.author","Klimova, Mariia"],["dc.contributor.author","Wills, Norma M."],["dc.contributor.author","Coakley, Arthur"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","O'Connor, Patrick B.F."],["dc.contributor.author","Loughran, Gary"],["dc.contributor.author","Weissman, Jonathan S."],["dc.contributor.author","Baranov, Pavel V."],["dc.contributor.author","Atkins, John F."],["dc.date.accessioned","2022-03-01T11:45:13Z"],["dc.date.available","2022-03-01T11:45:13Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1016/j.jmb.2020.05.010"],["dc.identifier.pii","S0022283620303466"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103253"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0022-2836"],["dc.title","Polysomes Bypass a 50-Nucleotide Coding Gap Less Efficiently Than Monosomes Due to Attenuation of a 5′ mRNA Stem–Loop and Enhanced Drop-off"],["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"]]