Rodnina, Marina V.

[["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Mercier, Evan"],["dc.contributor.author","Wintermeyer, Wolfgang"],["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","2020"],["dc.description.abstract","Integral membrane proteins insert into the bacterial inner membrane co-translationally via the translocon. Transmembrane (TM) segments of nascent proteins adopt their native topological arrangement with the N-terminus of the first TM (TM1) oriented to the outside (type I) or the inside (type II) of the cell. Here, we study TM1 topogenesis during ongoing translation in a bacterial in vitro system, applying real-time FRET and protease protection assays. We find that TM1 of the type I protein LepB reaches the translocon immediately upon emerging from the ribosome. In contrast, the type II protein EmrD requires a longer nascent chain before TM1 reaches the translocon and adopts its topology by looping inside the ribosomal peptide exit tunnel. Looping presumably is mediated by interactions between positive charges at the N-terminus of TM1 and negative charges in the tunnel wall. Early TM1 inversion is abrogated by charge reversal at the N-terminus. Kinetic analysis also shows that co-translational membrane insertion of TM1 is intrinsically rapid and rate-limited by translation. Thus, the ribosome has an important role in membrane protein topogenesis."],["dc.identifier.doi","10.15252/embj.2019104054"],["dc.identifier.pmid","32311161"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102986"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/112"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P16: Co-translationaler Einbau von Proteinen in die bakterielle Plasmamembran"],["dc.relation.eissn","1460-2075"],["dc.relation.issn","0261-4189"],["dc.relation.workinggroup","RG Rodnina"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Co‐translational insertion and topogenesis of bacterial membrane proteins monitored in real time"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","11858"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Nucleic acids research"],["dc.bibliographiccitation.lastpage","11866"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Mercier, Evan"],["dc.contributor.author","Holtkamp, Wolf"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2018-01-17T12:49:58Z"],["dc.date.available","2018-01-17T12:49:58Z"],["dc.date.issued","2017-11-16"],["dc.description.abstract","The bacterial signal recognition particle (SRP) is part of the machinery that targets ribosomes synthesizing membrane proteins to membrane-embedded translocons co-translationally. Recognition of nascent membrane proteins occurs by virtue of a hydrophobic signal-anchor sequence (SAS) contained in the nascent chain, usually at the N terminus. Here we use fluorescence-based stopped-flow to monitor SRP-ribosome interactions with actively translating ribosomes while an SRP substrate is synthesized and emerges from the peptide exit tunnel. The kinetic analysis reveals that, at cellular concentrations of ribosomes and SRP, SRP rapidly binds to translating ribosomes prior to the emergence of an SAS and forms an initial complex that rapidly rearranges to a more stable engaged complex. When the growing peptide reaches a length of ∼50 amino acids and the SAS is partially exposed, SRP undergoes another conformational change which further stabilizes the complex and initiates targeting of the translating ribosome to the translocon. These results provide a reconciled view on the timing of high-affinity targeting complex formation, while emphasizing the existence of preceding SRP recruitment steps under conditions of ongoing translation."],["dc.identifier.doi","10.1093/nar/gkx888"],["dc.identifier.pmid","29149347"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11688"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/14"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P16: Co-translationaler Einbau von Proteinen in die bakterielle Plasmamembran"],["dc.relation.eissn","1362-4962"],["dc.relation.workinggroup","RG Rodnina"],["dc.rights","CC BY-NC 4.0"],["dc.title","Signal recognition particle binds to translating ribosomes before emergence of a signal anchor sequence"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","24457"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Bögeholz, Lena A. K."],["dc.contributor.author","Mercier, Evan"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-03-01T11:46:04Z"],["dc.date.available","2022-03-01T11:46:04Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Synthesis of bacterial proteins on the ribosome starts with a formylated methionine. Removal of the N-terminal formyl group is essential and is carried out by peptide deformylase (PDF). Deformylation occurs co-translationally, shortly after the nascent-chain emerges from the ribosomal exit tunnel, and is necessary to allow for further N-terminal processing. Here we describe the kinetic mechanism of deformylation by PDF of ribosome-bound nascent-chains and show that PDF binding to and dissociation from ribosomes is rapid, allowing for efficient scanning of formylated substrates in the cell. The rate-limiting step in the PDF mechanism is a conformational rearrangement of the nascent-chain that takes place after cleavage of the formyl group. Under conditions of ongoing translation, the nascent-chain is deformylated rapidly as soon as it becomes accessible to PDF. Following deformylation, the enzyme is slow in releasing the deformylated nascent-chain, thereby delaying further processing and potentially acting as an early chaperone that protects short nascent chains before they reach a length sufficient to recruit other protein biogenesis factors."],["dc.identifier.doi","10.1038/s41598-021-03969-3"],["dc.identifier.pii","3969"],["dc.identifier.pmid","34961771"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103549"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/165"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation.eissn","2045-2322"],["dc.relation.workinggroup","RG Rodnina"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Kinetic control of nascent protein biogenesis by peptide deformylase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]