Bohnsack, Markus T.

[["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","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","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"]]