Bohnsack, Markus T.

[["dc.bibliographiccitation.firstpage","e54084"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PLoS One"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Missbach, Sandra"],["dc.contributor.author","Weis, Benjamin L."],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.editor","Lafontaine, Denis"],["dc.date.accessioned","2022-03-01T11:44:11Z"],["dc.date.available","2022-03-01T11:44:11Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1371/journal.pone.0054084"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102952"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1932-6203"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","40S Ribosome Biogenesis Co-Factors Are Essential for Gametophyte and Embryo Development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","583"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Cell"],["dc.bibliographiccitation.lastpage","592"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Granneman, Sander"],["dc.contributor.author","Ruprecht, Maike"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Tollervey, David"],["dc.date.accessioned","2022-03-01T11:45:16Z"],["dc.date.available","2022-03-01T11:45:16Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1016/j.molcel.2009.09.039"],["dc.identifier.pii","S1097276509006996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103272"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1097-2765"],["dc.title","Prp43 Bound at Different Sites on the Pre-rRNA Performs Distinct Functions in Ribosome Synthesis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Straub, Annika U."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Ruprecht, Maike"],["dc.contributor.author","Simm, S."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Bohnsack, M."],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:20:12Z"],["dc.date.available","2018-11-07T09:20:12Z"],["dc.date.issued","2013"],["dc.format.extent","100"],["dc.identifier.isi","000327927400151"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28829"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","RNA helicase function in yeast ribosome biogenesis"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","47"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biomolecular NMR Assignments"],["dc.bibliographiccitation.lastpage","50"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Veith, Thomas"],["dc.contributor.author","Wurm, Jan Philip"],["dc.contributor.author","Duchardt-Ferner, Elke"],["dc.contributor.author","Weis, Benjamin"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Safferthal, Charlotta"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Wöhnert, Jens"],["dc.date.accessioned","2022-03-01T11:44:39Z"],["dc.date.available","2022-03-01T11:44:39Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1007/s12104-011-9323-4"],["dc.identifier.pii","9323"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103078"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1874-270X"],["dc.relation.issn","1874-2718"],["dc.title","Backbone and side chain NMR resonance assignments for an archaeal homolog of the endonuclease Nob1 involved in ribosome biogenesis"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","5383"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Brüning, Lukas"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Davila Gallesio, Jimena"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2019-07-09T11:50:53Z"],["dc.date.available","2019-07-09T11:50:53Z"],["dc.date.issued","2018"],["dc.description.abstract","Production of eukaryotic ribosomal subunits is a highly dynamic process; pre-ribosomes undergo numerous structural rearrangements that establish the architecture present in mature complexes and serve as key checkpoints, ensuring the fidelity of ribosome assembly. Using in vivo crosslinking, we here identify the pre-ribosomal binding sites of three RNA helicases. Our data support roles for Has1 in triggering release of the U14 snoRNP, a critical event during early 40S maturation, and in driving assembly of domain I of pre-60S complexes. Binding of Mak5 to domain II of pre-60S complexes promotes recruitment of the ribosomal protein Rpl10, which is necessary for subunit joining and ribosome function. Spb4 binds to a molecular hinge at the base of ES27 facilitating binding of the export factor Arx1, thereby promoting pre-60S export competence. Our data provide important insights into the driving forces behind key structural remodelling events during ribosomal subunit assembly."],["dc.identifier.doi","10.1038/s41467-018-07783-w"],["dc.identifier.pmid","30568249"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16022"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59850"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/48"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P14: Die Rolle humaner Nucleoporine in Biogenese und Export makromolekularer Komplexe"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","610"],["dc.title","RNA helicases mediate structural transitions and compositional changes in pre-ribosomal complexes"],["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","4"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","18"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Straub, Annika U."],["dc.contributor.author","Doebele, Carmen"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:30:25Z"],["dc.date.available","2018-11-07T09:30:25Z"],["dc.date.issued","2013"],["dc.description.abstract","Ribosome synthesis requires a multitude of cofactors, among them DExD/H-box RNA helicases. Bacterial RNA helicases involved in ribosome assembly are not essential, while eukaryotes strictly require multiple DExD/H-box proteins that are involved in the much more complex ribosome biogenesis pathway. Here, RNA helicases are thought to act in structural remodeling of the RNPs including the modulation of protein binding, and they are required for allowing access or the release of specific snoRNPs from pre-ribosomes. Interestingly, helicase action is modulated by specific cofactors that can regulate recruitment and enzymatic activity. This review summarizes the current knowledge and focuses on recent findings and open questions on RNA helicase function and regulation in ribosome synthesis."],["dc.identifier.doi","10.4161/rna.21879"],["dc.identifier.isi","000314452200003"],["dc.identifier.pmid","22922795"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31303"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1547-6286"],["dc.title","DExD/H-box RNA helicases in ribosome biogenesis"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1173"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1182"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Ruprecht, Maike"],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Bruening, Lukas"],["dc.contributor.author","Mirus, Oliver"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Kudla, Grzegorz"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:37:25Z"],["dc.date.available","2018-11-07T09:37:25Z"],["dc.date.issued","2014"],["dc.description.abstract","Ribosome biogenesis in yeast requires 75 small nucleolar RNAs (snoRNAs) and a myriad of cofactors for processing, modification, and folding of the ribosomal RNAs (rRNAs). For the 19 RNA helicases implicated in ribosome synthesis, their sites of action and molecular functions have largely remained unknown. Here, we have used UV cross-linking and analysis of cDNA (CRAC) to reveal the pre-rRNA binding sites of the RNA helicase Rok1, which is involved in early small subunit biogenesis. Several contact sites were identified in the 18S rRNA sequence, which interestingly all cluster in the \"foot\" region of the small ribosomal subunit. These include a major binding site in the eukaryotic expansion segment ES6, where Rok1 is required for release of the snR30 snoRNA. Rok1 directly contacts snR30 and other snoRNAs required for pre-rRNA processing. Using cross-linking, ligation and sequencing of hybrids (CLASH) we identified several novel pre-rRNA base-pairing sites for the snoRNAs snR30, snR10, U3, and U14, which cluster in the expansion segments of the 18S rRNA. Our data suggest that these snoRNAs bridge interactions between the expansion segments, thereby forming an extensive interaction network that likely promotes pre-rRNA maturation and folding in early pre-ribosomal complexes and establishes long-range rRNA interactions during ribosome synthesis."],["dc.identifier.doi","10.1261/rna.044669.114"],["dc.identifier.isi","000339176800002"],["dc.identifier.pmid","24947498"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32835"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.issn","1469-9001"],["dc.relation.issn","1355-8382"],["dc.title","A pre-ribosomal RNA interaction network involving snoRNAs and the Rok1 helicase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","599"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biological Chemistry"],["dc.bibliographiccitation.lastpage","604"],["dc.bibliographiccitation.volume","393"],["dc.contributor.author","Leisegang, Matthias S."],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Ramirez, Ana S."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:08:30Z"],["dc.date.available","2018-11-07T09:08:30Z"],["dc.date.issued","2012"],["dc.description.abstract","The biogenesis of most eukaryotic kinds of RNA requires nuclear export, which is mediated by a variety of specific nuclear transport receptors. The nuclear export receptors Exportin-t (Exp-t) and Exportin 5 (Exp5), and their homologues, are involved in the export of transfer RNA to the cytoplasm. Exp5 is further involved in additional nucleocytoplasmic transport pathways, which include nuclear export of microRNA precursors (pre-miRNAs) and pre-60S ribosomal subunits. Inactivation of Exp5 results in nuclear accumulation of pre-miRNAs and perturbation of gene expression, and its mutation was recently found in malignant diseases. Here, we compare the cellular function of Exp5 and Exp-t with focus on Exp5 substrates and its role in diseases."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [BO3442/1-1]"],["dc.identifier.doi","10.1515/hsz-2012-0146"],["dc.identifier.isi","000307087600006"],["dc.identifier.pmid","22944664"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10599"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/26048"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Walter De Gruyter & Co"],["dc.relation.issn","1431-6730"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Exportin T and Exportin 5: tRNA and miRNA biogenesis - and beyond"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3259"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","3274"],["dc.bibliographiccitation.volume","40"],["dc.contributor.author","Veith, Thomas"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Wurm, Jan P."],["dc.contributor.author","Weis, Benjamin L."],["dc.contributor.author","Duchardt-Ferner, Elke"],["dc.contributor.author","Safferthal, Charlotta"],["dc.contributor.author","Hennig, Raoul"],["dc.contributor.author","Mirus, Oliver"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Wöhnert, Jens"],["dc.contributor.author","Schleiff, Enrico"],["dc.date.accessioned","2022-03-01T11:46:48Z"],["dc.date.available","2022-03-01T11:46:48Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1093/nar/gkr1186"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103805"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","Structural and functional analysis of the archaeal endonuclease Nob1"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4066"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","4084"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Krogh, Nicolai"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Martin, Roman"],["dc.contributor.author","Gallesio, Jimena Davila"],["dc.contributor.author","van Nues, Robert W."],["dc.contributor.author","Schneider, Claudia"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Nielsen, Henrik"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-07-05T14:57:35Z"],["dc.date.available","2021-07-05T14:57:35Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract RNA helicases play important roles in diverse aspects of RNA metabolism through their functions in remodelling ribonucleoprotein complexes (RNPs), such as pre-ribosomes. Here, we show that the DEAD box helicase Dbp3 is required for efficient processing of the U18 and U24 intron-encoded snoRNAs and 2′-O-methylation of various sites within the 25S ribosomal RNA (rRNA) sequence. Furthermore, numerous box C/D snoRNPs accumulate on pre-ribosomes in the absence of Dbp3. Many snoRNAs guiding Dbp3-dependent rRNA modifications have overlapping pre-rRNA basepairing sites and therefore form mutually exclusive interactions with pre-ribosomes. Analysis of the distribution of these snoRNAs between pre-ribosome-associated and \\‘free\\’ pools demonstrated that many are almost exclusively associated with pre-ribosomal complexes. Our data suggest that retention of such snoRNPs on pre-ribosomes when Dbp3 is lacking may impede rRNA 2′-O-methylation by reducing the recycling efficiency of snoRNPs and by inhibiting snoRNP access to proximal target sites. The observation of substoichiometric rRNA modification at adjacent sites suggests that the snoRNPs guiding such modifications likely interact stochastically rather than hierarchically with their pre-rRNA target sites. Together, our data provide new insights into the dynamics of snoRNPs on pre-ribosomal complexes and the remodelling events occurring during the early stages of ribosome assembly."],["dc.description.abstract","Abstract RNA helicases play important roles in diverse aspects of RNA metabolism through their functions in remodelling ribonucleoprotein complexes (RNPs), such as pre-ribosomes. Here, we show that the DEAD box helicase Dbp3 is required for efficient processing of the U18 and U24 intron-encoded snoRNAs and 2′-O-methylation of various sites within the 25S ribosomal RNA (rRNA) sequence. Furthermore, numerous box C/D snoRNPs accumulate on pre-ribosomes in the absence of Dbp3. Many snoRNAs guiding Dbp3-dependent rRNA modifications have overlapping pre-rRNA basepairing sites and therefore form mutually exclusive interactions with pre-ribosomes. Analysis of the distribution of these snoRNAs between pre-ribosome-associated and ‘free’ pools demonstrated that many are almost exclusively associated with pre-ribosomal complexes. Our data suggest that retention of such snoRNPs on pre-ribosomes when Dbp3 is lacking may impede rRNA 2′-O-methylation by reducing the recycling efficiency of snoRNPs and by inhibiting snoRNP access to proximal target sites. The observation of substoichiometric rRNA modification at adjacent sites suggests that the snoRNPs guiding such modifications likely interact stochastically rather than hierarchically with their pre-rRNA target sites. Together, our data provide new insights into the dynamics of snoRNPs on pre-ribosomal complexes and the remodelling events occurring during the early stages of ribosome assembly."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1093/nar/gkab159"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87680"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-441"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.relation.orgunit","Institut für Molekularbiologie"],["dc.rights","CC BY-NC 4.0"],["dc.title","RNA helicase-mediated regulation of snoRNP dynamics on pre-ribosomes and rRNA 2′- O -methylation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]