Rodnina, Marina V.

[["dc.bibliographiccitation.artnumber","871121"],["dc.bibliographiccitation.journal","Frontiers in Molecular Biosciences"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Mercier, Evan"],["dc.contributor.author","Wang, Xiaolin"],["dc.contributor.author","Bögeholz, Lena A. K."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2022-06-01T09:39:51Z"],["dc.date.available","2022-06-01T09:39:51Z"],["dc.date.issued","2022"],["dc.description.abstract","Nascent polypeptides emerging from the ribosome during translation are rapidly scanned and processed by ribosome-associated protein biogenesis factors (RPBs). RPBs cleave the N-terminal formyl and methionine groups, assist cotranslational protein folding, and sort the proteins according to their cellular destination. Ribosomes translating inner-membrane proteins are recognized and targeted to the translocon with the help of the signal recognition particle, SRP, and SRP receptor, FtsY. The growing nascent peptide is then inserted into the phospholipid bilayer at the translocon, an inner-membrane protein complex consisting of SecY, SecE, and SecG. Folding of membrane proteins requires that transmembrane helices (TMs) attain their correct topology, the soluble domains are inserted at the correct (cytoplasmic or periplasmic) side of the membrane, and – for polytopic membrane proteins – the TMs find their interaction partner TMs in the phospholipid bilayer. This review describes the recent progress in understanding how growing nascent peptides are processed and how inner-membrane proteins are targeted to the translocon and find their correct orientation at the membrane, with the focus on biophysical approaches revealing the dynamics of the process. We describe how spontaneous fluctuations of the translocon allow diffusion of TMs into the phospholipid bilayer and argue that the ribosome orchestrates cotranslational targeting not only by providing the binding platform for the RPBs or the translocon, but also by helping the nascent chains to find their correct orientation in the membrane. Finally, we present the auxiliary role of YidC as a chaperone for inner-membrane proteins. We show how biophysical approaches provide new insights into the dynamics of membrane protein biogenesis and raise new questions as to how translation modulates protein folding."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship"," European Research Council"],["dc.identifier.doi","10.3389/fmolb.2022.871121"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108581"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","2296-889X"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Cotranslational Biogenesis of Membrane Proteins in Bacteria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","380"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Analytical Biochemistry"],["dc.bibliographiccitation.lastpage","381"],["dc.bibliographiccitation.volume","219"],["dc.contributor.author","Rodnina, Marina V."],["dc.contributor.author","Semenkov, Y.P."],["dc.contributor.author","Wintermeyer, W."],["dc.date.accessioned","2022-03-01T11:46:52Z"],["dc.date.available","2022-03-01T11:46:52Z"],["dc.date.issued","1994"],["dc.identifier.doi","10.1006/abio.1994.1282"],["dc.identifier.pii","S0003269784712826"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103826"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0003-2697"],["dc.title","Purification of fMET-tRNAfMET by Fast Protein Liquid Chromatography"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","15408"],["dc.bibliographiccitation.issue","44"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","15413"],["dc.bibliographiccitation.volume","37"],["dc.contributor.author","Jagath, J. R."],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Lentzen, G."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:48:05Z"],["dc.date.available","2017-09-07T11:48:05Z"],["dc.date.issued","1998"],["dc.description.abstract","The bacterial signal recognition particle (SRP) is an RNA-protein complex. In Escherichia coli, the particle consists of a 114 nt RNA, a 4.5S RNA, and a 48 kDa GTP-binding protein, Ffh. GDP-GTP exchange on, and GTP hydrolysis by, Ffh are thought to regulate SRP function in membrane targeting of translating ribosomes. In the present paper, we report the equilibrium and kinetic constants of guanine nucleotide binding to Ffh in different functional complexes. The association and dissociation rate constants of GTP/GDP binding to Ffh were measured using a fluorescent analogue of GTP/GDP, mant-GTP/GDP. For both nucleotides, association and dissociation rate constants were about 10(6) M-1 s(-1) and 10 s(-1) respectively. The equilibrium constants of nonmodified GTP and GDP binding to Ffh alone and in SRP, and in the complex with the ribosomes were measured by competition with mant-GDP. In all cases, the same 1-2 mu M affinity for GTP and GDP was observed. Binding of both GTP and GDP to Ffh was independent of Mg2+ ions. The data suggest that, at conditions in vivo, (i) there will be rapid spontaneous GDP-GTP exchange, and (ii) the GTP-bound form of Ffh, or of SRP, will be predominant."],["dc.identifier.doi","10.1021/bi981523a"],["dc.identifier.gro","3144511"],["dc.identifier.isi","000076887400019"],["dc.identifier.pmid","9799502"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2143"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","Interaction of guanine nucleotides with the signal recognition particle from Escherichia coli"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","390"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","401"],["dc.bibliographiccitation.volume","69"],["dc.contributor.author","Lancaster, Lorna E."],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Kleanthous, Colin"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina V."],["dc.date.accessioned","2018-01-29T15:14:13Z"],["dc.date.available","2018-01-29T15:14:13Z"],["dc.date.issued","2008"],["dc.description.abstract","The cytotoxin colicin E3 targets the 30S subunit of bacterial ribosomes and specifically cleaves 16S rRNA at the decoding centre, thereby inhibiting translation. Although the cleavage site is well known, it is not clear which step of translation is inhibited. We studied the effects of colicin E3 cleavage on ribosome functions by analysing individual steps of protein synthesis. We find that the cleavage affects predominantly the elongation step. The inhibitory effect of colicin E3 cleavage originates from the accumulation of sequential impaired decoding events, each of which results in low occupancy of the A site and, consequently, decreasing yield of elongating peptide. The accumulation leads to an almost complete halt of translation after reading of a few codons. The cleavage of 16S rRNA does not impair monitoring of codon-anticodon complexes or GTPase activation during elongation-factor Tu-dependent binding of aminoacyl-tRNA, but decreases the stability of the codon-recognition complex and slows down aminoacyl-tRNA accommodation in the A site. The tRNA-mRNA translocation is faster on colicin E3-cleaved than on intact ribosomes and is less sensitive to inhibition by the antibiotic viomycin."],["dc.identifier.doi","10.1111/j.1365-2958.2008.06283.x"],["dc.identifier.pmid","18485067"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/11894"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1365-2958"],["dc.title","Colicin E3 cleavage of 16S rRNA impairs decoding and accelerates tRNA translocation on Escherichia coli ribosomes"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7237"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","7239"],["dc.bibliographiccitation.volume","95"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:48:09Z"],["dc.date.available","2017-09-07T11:48:09Z"],["dc.date.issued","1998"],["dc.identifier.doi","10.1073/pnas.95.13.7237"],["dc.identifier.gro","3144541"],["dc.identifier.isi","000074436400001"],["dc.identifier.pmid","9636131"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2176"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Form follows function: Structure of an elongation factor G-ribosome complex"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1183"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","1194"],["dc.bibliographiccitation.volume","343"],["dc.contributor.author","Peske, Frank"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Katunin, Vladimir I."],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:43:10Z"],["dc.date.available","2017-09-07T11:43:10Z"],["dc.date.issued","2004"],["dc.description.abstract","Translocation, a coordinated movement of two tRNAs together with mRNA on the ribosome, is catalyzed by elongation factor G (EF-G). The reaction is accompanied by conformational rearrangements of the ribosome that are, as yet, not well characterized. Here, we analyze those rearrangements by restricting the conformational flexibility of the ribosome by antibiotics binding to specific sites of the ribosome. Paromomycin (Par), viomycin (Vio), spectinomycin (Spc), and hygromycin B (HygB) inhibited the tRNA-mRNA movement, while the other partial reactions of translocation, including the unlocking rearrangement of the ribosome that precedes tRNA-mRNA movement, were not affected. The functional cycle of EF-G, i.e. binding of EF-G(.)GTP to the ribosome, GTP hydrolysis, Pi release, and dissociation of EF-G(.)GDP from the ribosome, was not affected either, indicating that EF-G turnover is not coupled directly to tRNA-mRNA movement. The inhibition of translocation. by Par and Vio is attributed to the stabilization of tRNA binding in the A site, whereas Spc and HygB had a direct inhibitory effect on tRNA-mRNA movement. Streptomycin (Str) had essentially no effect on translocation, although it caused a large increase in tRNA affinity to the A site. These results suggest that conformational changes in the vicinity of the decoding region at the binding sites of Spc and HygB are important for tRNA-mRNA movement, whereas Str seems to stabilize a conformation of the ribosome that is prone to rapid translocation, thereby compensating the effect on tRNA affinity. (C) 2004 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2004.08.097"],["dc.identifier.gro","3143929"],["dc.identifier.isi","000224838800003"],["dc.identifier.pmid","15491605"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1497"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA translocation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","450"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","459"],["dc.bibliographiccitation.volume","228"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.date.accessioned","2017-09-07T11:51:34Z"],["dc.date.available","2017-09-07T11:51:34Z"],["dc.date.issued","1992"],["dc.identifier.doi","10.1016/0022-2836(92)90834-7"],["dc.identifier.gro","3144786"],["dc.identifier.isi","A1992KA67600016"],["dc.identifier.pmid","1453456"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2448"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Academic Press Ltd"],["dc.relation.issn","0022-2836"],["dc.title","2 TRANSFER RNA-BINDING SITES IN ADDITION TO A-SITE AND P-SITE ON EUKARYOTIC RIBOSOMES"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","12520"],["dc.bibliographiccitation.issue","41"],["dc.bibliographiccitation.journal","Biochemistry"],["dc.bibliographiccitation.lastpage","12528"],["dc.bibliographiccitation.volume","41"],["dc.contributor.author","Mohr, Dagmar"],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Rodnina, Marina"],["dc.date.accessioned","2017-09-07T11:45:12Z"],["dc.date.available","2017-09-07T11:45:12Z"],["dc.date.issued","2002"],["dc.description.abstract","The GTPase activity of elongation factors Tu and G is stimulated by the ribosome. The factor binding site is located on the 50S ribosomal subunit and comprises proteins L7/12, L10, L11, the L11-binding region of 23S rRNA, and the sarcin-ricin loop of 239 rRNA. The role of these ribosomal elements in factor binding, GTPase activation, or functions in tRNA binding and translocation, and their relative contributions, is not known. By comparing ribosomes depleted of L7/12 and reconstituted ribosomes, we show that, for both factors, interactions with L7/12 and with other ribosomal residues contribute about equally and additively to GTPase activation, resulting in an overall 10(7)-fold stimulation. Removal of L7/12 has little effect on factor binding to the ribosome. Effects on other factor-dependent functions, i.e., A-site binding of aminoacyl-tRNA and translocation, are fully explained by the inhibition of GTP hydrolysis. Based on these results, we propose that L7/12 stimulates the GTPase activity of both factors by inducing the catalytically active conformation of the G domain. This effect appears to be augmented by interactions of other structural elements of the large ribosomal subunit with the switch regions of the factors."],["dc.identifier.doi","10.1021/bi026301y"],["dc.identifier.gro","3144163"],["dc.identifier.isi","000178494400030"],["dc.identifier.pmid","12369843"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/1757"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Amer Chemical Soc"],["dc.relation.issn","0006-2960"],["dc.title","GTPase activation of elongation factors Tu and G 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","301"],["dc.bibliographiccitation.lastpage","318"],["dc.contributor.author","Rodnina, Marina"],["dc.contributor.author","Matassova, Natalia B."],["dc.contributor.author","Wintermeyer, Wolfgang"],["dc.contributor.author","Savelsbergh, Andreas"],["dc.contributor.author","Pape, Tillmann"],["dc.contributor.author","Mohr, Dagmar"],["dc.contributor.editor","Garrett, Roger A."],["dc.date.accessioned","2017-09-07T11:54:06Z"],["dc.date.available","2017-09-07T11:54:06Z"],["dc.date.issued","2014"],["dc.description.abstract","This chapter concentrates on pre-steady-state kinetic work, and provides evidence on how much the interpretation of kinetic results in molecular-mechanistic terms owes to structural information obtained from crystallography and cryo-electron microscopy. Our studies of elongation factor (EF-Tu) function address two main issues: (i) the elucidation of the reaction pathway to identify intermediate steps of A-site binding and (ii) the quantitative evaluation of the pathway in order to understand specificity. Based on measured rates of GTP hydrolysis and peptide bond formation, Thompson and colleagues proposed that the rate of GTP hydrolysis by EF-Tu is independent of the tRNA, thereby providing an internal kinetic standard for translational accuracy. Binding of thiostrepton to the 1070 region of 23S rRNA interferes with translocation, as it strongly inhibits Pi release, translocation, and subsequent turnover of EF-G; in contrast, EF-G binding and GTP hydrolysis are not affected. The GTPase activities of EF-Tu and EF-G intrinsically are very low and are strongly enhanced on the ribosome. Recently, the ability of isolated L12 protein to stimulate GTP hydrolysis by either EF-Tu or EF-G, has been studied. In the fusidic acid-stabilized complex of EF-G with the ribosome, the α- sarcin stem is close to position 196 in the G domain of EF-G, which lies just above the GTP binding site, while the α-sarcin loop region is in the vicinity of position 650 in domain 5 of the factor."],["dc.identifier.doi","10.1128/9781555818142.ch25"],["dc.identifier.gro","3145105"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2805"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.publisher","American Society for Microbiology Press"],["dc.publisher.place","Washington, DC"],["dc.relation.doi","10.1128/9781555818142"],["dc.relation.isbn","1-55581-184-1"],["dc.relation.isbn","978-1-55581-184-6"],["dc.relation.ispartof","The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions"],["dc.title","Mechanisms of Partial Reactions of the Elongation Cycle Catalyzed by Elongation Factors Tu and G"],["dc.type","book_chapter"],["dc.type.internalPublication","no"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["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"]]