Samatova, Ekaterina N.

[["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","97"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Liutkute, Marija"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:44:24Z"],["dc.date.available","2022-03-01T11:44:24Z"],["dc.date.issued","2020"],["dc.description.abstract","Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways. In this review, we summarize the recent examples of how translation affects folding of single-domain, multiple-domain and oligomeric proteins. The vectorial nature of translation, the spatial constraints of the exit tunnel, and the electrostatic properties of the ribosome-nascent peptide complex define the onset of early folding events. The ribosome can facilitate protein compaction, induce the formation of intermediates that are not observed in solution, or delay the onset of folding. Examples of single-domain proteins suggest that early compaction events can define the folding pathway for some types of domain structures. Folding of multi-domain proteins proceeds in a domain-wise fashion, with each domain having its role in stabilizing or destabilizing neighboring domains. Finally, the assembly of protein complexes can also begin cotranslationally. In all these cases, the ribosome helps the nascent protein to attain a native fold and avoid the kinetic traps of misfolding."],["dc.description.abstract","Many proteins in the cell fold cotranslationally within the restricted space of the polypeptide exit tunnel or at the surface of the ribosome. A growing body of evidence suggests that the ribosome can alter the folding trajectory in many different ways. In this review, we summarize the recent examples of how translation affects folding of single-domain, multiple-domain and oligomeric proteins. The vectorial nature of translation, the spatial constraints of the exit tunnel, and the electrostatic properties of the ribosome-nascent peptide complex define the onset of early folding events. The ribosome can facilitate protein compaction, induce the formation of intermediates that are not observed in solution, or delay the onset of folding. Examples of single-domain proteins suggest that early compaction events can define the folding pathway for some types of domain structures. Folding of multi-domain proteins proceeds in a domain-wise fashion, with each domain having its role in stabilizing or destabilizing neighboring domains. Finally, the assembly of protein complexes can also begin cotranslationally. In all these cases, the ribosome helps the nascent protein to attain a native fold and avoid the kinetic traps of misfolding."],["dc.identifier.doi","10.3390/biom10010097"],["dc.identifier.pii","biom10010097"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103017"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","2218-273X"],["dc.title","Cotranslational Folding of Proteins on the Ribosome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Agirrezabala, Xabier"],["dc.contributor.author","Samatova, Ekaterina"],["dc.contributor.author","Macher, Meline"],["dc.contributor.author","Liutkute, Marija"],["dc.contributor.author","Maiti, Manisankar"],["dc.contributor.author","Gil‐Carton, David"],["dc.contributor.author","Novacek, Jiri"],["dc.contributor.author","Valle, Mikel"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:44:18Z"],["dc.date.available","2022-03-01T11:44:18Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.15252/embj.2021109175"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102988"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.title","A switch from α‐helical to β‐strand conformation during co‐translational protein folding"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]