Bohnsack, Markus T.

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Birikmen, Mehmet"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Tran, Vinh"],["dc.contributor.author","Somayaji, Sharvari"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Ebersberger, Ingo"],["dc.date.accessioned","2021-12-01T09:24:03Z"],["dc.date.available","2021-12-01T09:24:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Ribosome assembly is an essential and carefully choreographed cellular process. In eukaryotes, several 100 proteins, distributed across the nucleolus, nucleus, and cytoplasm, co-ordinate the step-wise assembly of four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins (RPs) into the mature ribosomal subunits. Due to the inherent complexity of the assembly process, functional studies identifying ribosome biogenesis factors and, more importantly, their precise functions and interplay are confined to a few and very well-established model organisms. Although best characterized in yeast ( Saccharomyces cerevisiae ), emerging links to disease and the discovery of additional layers of regulation have recently encouraged deeper analysis of the pathway in human cells. In archaea, ribosome biogenesis is less well-understood. However, their simpler sub-cellular structure should allow a less elaborated assembly procedure, potentially providing insights into the functional essentials of ribosome biogenesis that evolved long before the diversification of archaea and eukaryotes. Here, we use a comprehensive phylogenetic profiling setup, integrating targeted ortholog searches with automated scoring of protein domain architecture similarities and an assessment of when search sensitivity becomes limiting, to trace 301 curated eukaryotic ribosome biogenesis factors across 982 taxa spanning the tree of life and including 727 archaea. We show that both factor loss and lineage-specific modifications of factor function modulate ribosome biogenesis, and we highlight that limited sensitivity of the ortholog search can confound evolutionary conclusions. Projecting into the archaeal domain, we find that only few factors are consistently present across the analyzed taxa, and lineage-specific loss is common. While members of the Asgard group are not special with respect to their inventory of ribosome biogenesis factors (RBFs), they unite the highest number of orthologs to eukaryotic RBFs in one taxon. Using large ribosomal subunit maturation as an example, we demonstrate that archaea pursue a simplified version of the corresponding steps in eukaryotes. Much of the complexity of this process evolved on the eukaryotic lineage by the duplication of ribosomal proteins and their subsequent functional diversification into ribosome biogenesis factors. This highlights that studying ribosome biogenesis in archaea provides fundamental information also for understanding the process in eukaryotes."],["dc.description.abstract","Ribosome assembly is an essential and carefully choreographed cellular process. In eukaryotes, several 100 proteins, distributed across the nucleolus, nucleus, and cytoplasm, co-ordinate the step-wise assembly of four ribosomal RNAs (rRNAs) and approximately 80 ribosomal proteins (RPs) into the mature ribosomal subunits. Due to the inherent complexity of the assembly process, functional studies identifying ribosome biogenesis factors and, more importantly, their precise functions and interplay are confined to a few and very well-established model organisms. Although best characterized in yeast ( Saccharomyces cerevisiae ), emerging links to disease and the discovery of additional layers of regulation have recently encouraged deeper analysis of the pathway in human cells. In archaea, ribosome biogenesis is less well-understood. However, their simpler sub-cellular structure should allow a less elaborated assembly procedure, potentially providing insights into the functional essentials of ribosome biogenesis that evolved long before the diversification of archaea and eukaryotes. Here, we use a comprehensive phylogenetic profiling setup, integrating targeted ortholog searches with automated scoring of protein domain architecture similarities and an assessment of when search sensitivity becomes limiting, to trace 301 curated eukaryotic ribosome biogenesis factors across 982 taxa spanning the tree of life and including 727 archaea. We show that both factor loss and lineage-specific modifications of factor function modulate ribosome biogenesis, and we highlight that limited sensitivity of the ortholog search can confound evolutionary conclusions. Projecting into the archaeal domain, we find that only few factors are consistently present across the analyzed taxa, and lineage-specific loss is common. While members of the Asgard group are not special with respect to their inventory of ribosome biogenesis factors (RBFs), they unite the highest number of orthologs to eukaryotic RBFs in one taxon. Using large ribosomal subunit maturation as an example, we demonstrate that archaea pursue a simplified version of the corresponding steps in eukaryotes. Much of the complexity of this process evolved on the eukaryotic lineage by the duplication of ribosomal proteins and their subsequent functional diversification into ribosome biogenesis factors. This highlights that studying ribosome biogenesis in archaea provides fundamental information also for understanding the process in eukaryotes."],["dc.identifier.doi","10.3389/fmicb.2021.739000"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94834"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-302X"],["dc.rights","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Tracing Eukaryotic Ribosome Biogenesis Factors Into the Archaeal Domain Sheds Light on the Evolution of Functional Complexity"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","237"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","247"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Watkins, Nicholas J."],["dc.date.accessioned","2018-11-07T09:19:15Z"],["dc.date.available","2018-11-07T09:19:15Z"],["dc.date.issued","2013"],["dc.description.abstract","Several proto-oncogenes and tumor suppressors regulate the production of ribosomes. Ribosome biogenesis is a major consumer of cellular energy, and defects result in p53 activation via repression of mouse double minute 2 (MDM2) homolog by the ribosomal proteins RPL5 and RPL11. Here, we report that RPL5 and RPL11 regulate p53 from the context of a ribosomal subcomplex, the 5S ribonucleoprotein particle (RNP). We provide evidence that the third component of this complex, the 5S rRNA, is critical for p53 regulation. In addition, we show that the 5S RNP is essential for the activation of p53 by p14(ARF), a protein that is activated by oncogene overexpression. Our data show that the abundance of the 5S RNP, and therefore p53 levels, is determined by factors regulating 5S complex formation and ribosome integration, including the tumor suppressor PICT1. The 5S RNP therefore emerges as the critical coordinator of signaling pathways that couple cell proliferation with ribosome production."],["dc.identifier.doi","10.1016/j.celrep.2013.08.049"],["dc.identifier.isi","000326152100024"],["dc.identifier.pmid","24120868"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10667"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28592"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The 5S RNP Couples p53 Homeostasis to Ribosome Biogenesis and Nucleolar Stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2329"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","2340"],["dc.bibliographiccitation.volume","217"],["dc.contributor.author","Aksu, Metin"],["dc.contributor.author","Pleiner, Tino"],["dc.contributor.author","Karaca, Samir"],["dc.contributor.author","Kappert, Christin"],["dc.contributor.author","Dehne, Heinz-Jürgen"],["dc.contributor.author","Seibel, Katharina"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Görlich, Dirk"],["dc.date.accessioned","2019-03-20T13:49:37Z"],["dc.date.available","2019-03-20T13:49:37Z"],["dc.date.issued","2018"],["dc.description.abstract","Exportins bind cargo molecules in a RanGTP-dependent manner inside nuclei and transport them through nuclear pores to the cytoplasm. CRM1/Xpo1 is the best-characterized exportin because specific inhibitors such as leptomycin B allow straightforward cargo validations in vivo. The analysis of other exportins lagged far behind, foremost because no such inhibitors had been available for them. In this study, we explored the cargo spectrum of exportin 7/Xpo7 in depth and identified not only ∼200 potential export cargoes but also, surprisingly, ∼30 nuclear import substrates. Moreover, we developed anti-Xpo7 nanobodies that acutely block Xpo7 function when transfected into cultured cells. The inhibition is pathway specific, mislocalizes export cargoes of Xpo7 to the nucleus and import substrates to the cytoplasm, and allowed validation of numerous tested cargo candidates. This establishes Xpo7 as a broad-spectrum bidirectional transporter and paves the way for a much deeper analysis of exportin and importin function in the future."],["dc.identifier.doi","10.1083/jcb.201712013"],["dc.identifier.pmid","29748336"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/57682"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/30"],["dc.language.iso","en"],["dc.notes.status","final"],["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","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Görlich (Cellular Logistics)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","Xpo7 is a broad-spectrum exportin and a nuclear import receptor"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Trends in Biochemical Sciences"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Kleiber, Nicole"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-04-06T07:33:28Z"],["dc.date.available","2022-04-06T07:33:28Z"],["dc.date.issued","2022-03-29"],["dc.description.abstract","Modified nucleotides within cellular RNAs significantly influence their biogenesis, stability, and function. As reviewed here, 3-methylcytidine (m3C) has recently come to the fore through the identification of the methyltransferases responsible for installing m3C32 in human tRNAs. Mechanistic details of how m3C32 methyltransferases recognize their substrate tRNAs have been uncovered and the biogenetic and functional relevance of interconnections between m3C32 and modified adenosines at position 37 highlighted. Functional insights into the role of m3C32 modifications indicate that they influence tRNA structure and, consistently, lack of m3C32 modifications impairs translation. Development of quantitative, transcriptome-wide m3C mapping approaches and the discovery of an m3C demethylase reveal m3C to be dynamic, raising the possibility that it contributes to fine-tuning gene expression in different conditions."],["dc.identifier.doi","10.1016/j.tibs.2022.03.004"],["dc.identifier.pmid","35365384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/106432"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/468"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/174"],["dc.language.iso","en"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.issn","0968-0004"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Roles and dynamics of 3-methylcytidine in cellular RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1009407"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Pätz, Christina"],["dc.contributor.author","Akkermann, Dagmar"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Galka, Dajana"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-04-14T08:28:05Z"],["dc.date.available","2021-04-14T08:28:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1371/journal.pgen.1009407"],["dc.identifier.pmid","33657088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82500"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/140"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY 4.0"],["dc.title","DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization"],["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","5824"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","5837.e15"],["dc.bibliographiccitation.volume","184"],["dc.contributor.author","Cruz-Zaragoza, Luis Daniel"],["dc.contributor.author","Dennerlein, Sven"],["dc.contributor.author","Linden, Andreas"],["dc.contributor.author","Yousefi, Roya"],["dc.contributor.author","Lavdovskaia, Elena"],["dc.contributor.author","Aich, Abhishek"],["dc.contributor.author","Falk, Rebecca R."],["dc.contributor.author","Gomkale, Ridhima"],["dc.contributor.author","Schöndorf, Thomas"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2021-12-01T09:23:52Z"],["dc.date.available","2021-12-01T09:23:52Z"],["dc.date.issued","2021"],["dc.description.abstract","The human mitochondrial genome encodes thirteen core subunits of the oxidative phosphorylation system, and defects in mitochondrial gene expression lead to severe neuromuscular disorders. However, the mechanisms of mitochondrial gene expression remain poorly understood due to a lack of experimental approaches to analyze these processes. Here, we present an in vitro system to silence translation in purified mitochondria. In vitro import of chemically synthesized precursor-morpholino hybrids allows us to target translation of individual mitochondrial mRNAs. By applying this approach, we conclude that the bicistronic, overlapping ATP8/ATP6 transcript is translated through a single ribosome/mRNA engagement. We show that recruitment of COX1 assembly factors to translating ribosomes depends on nascent chain formation. By defining mRNA-specific interactomes for COX1 and COX2, we reveal an unexpected function of the cytosolic oncofetal IGF2BP1, an RNA-binding protein, in mitochondrial translation. Our data provide insight into mitochondrial translation and innovative strategies to investigate mitochondrial gene expression."],["dc.identifier.doi","10.1016/j.cell.2021.09.033"],["dc.identifier.pii","S0092867421011168"],["dc.identifier.pmid","34672953"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94777"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/355"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/161"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation.issn","0092-8674"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.title","An in vitro system to silence mitochondrial gene expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","6152"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Aquino, Gerald Ryan R."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Krogh, Nicolai"],["dc.contributor.author","Pan, Kuan-Ting"],["dc.contributor.author","Jaafar, Mariam"],["dc.contributor.author","Henras, Anthony K."],["dc.contributor.author","Nielsen, Henrik"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-12-01T09:20:51Z"],["dc.date.available","2021-12-01T09:20:51Z"],["dc.date.issued","2021"],["dc.description.abstract","Early pre-60S ribosomal particles are poorly characterized, highly dynamic complexes that undergo extensive rRNA folding and compaction concomitant with assembly of ribosomal proteins and exchange of assembly factors. Pre-60S particles contain numerous RNA helicases, which are likely regulators of accurate and efficient formation of appropriate rRNA structures. Here we reveal binding of the RNA helicase Dbp7 to domain V/VI of early pre-60S particles in yeast and show that in the absence of this protein, dissociation of the Npa1 scaffolding complex, release of the snR190 folding chaperone, recruitment of the A3 cluster factors and binding of the ribosomal protein uL3 are impaired. uL3 is critical for formation of the peptidyltransferase center (PTC) and is responsible for stabilizing interactions between the 5′ and 3′ ends of the 25S, an essential pre-requisite for subsequent pre-60S maturation events. Highlighting the importance of pre-ribosome remodeling by Dbp7, our data suggest that in the absence of Dbp7 or its catalytic activity, early pre-ribosomal particles are targeted for degradation."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41467-021-26208-9"],["dc.identifier.pii","26208"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94285"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2041-1723"],["dc.rights","CC BY 4.0"],["dc.title","The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","8074"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","8089"],["dc.bibliographiccitation.volume","48"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Ferreira, Rafael Rinaldi"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Gruber, Jens"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-04-14T08:24:14Z"],["dc.date.available","2021-04-14T08:24:14Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1093/nar/gkaa549"],["dc.identifier.pmid","32609813"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17489"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81210"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/53"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/116"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["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.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","The human box C/D snoRNA U3 is a miRNA source and miR-U3 regulates expression of sortin nexin 27"],["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","553"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","564"],["dc.bibliographiccitation.volume","43"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Leisegang, Matthias S."],["dc.contributor.author","Doebele, Carmen"],["dc.contributor.author","Ramirez, Ana S."],["dc.contributor.author","Simm, Stefan"],["dc.contributor.author","Safferthal, Charlotta"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Schorge, Tobias"],["dc.contributor.author","Markoutsa, Stavroula"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Karas, Michael"],["dc.contributor.author","Ebersberger, Ingo"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T10:03:32Z"],["dc.date.available","2018-11-07T10:03:32Z"],["dc.date.issued","2015"],["dc.description.abstract","Translation fidelity and efficiency require multiple ribosomal (r)RNA modifications that are mostly mediated by small nucleolar (sno)RNPs during ribosome production. Overlapping basepairing of snoRNAs with pre-rRNAs often necessitates sequential and efficient association and dissociation of the snoRNPs, however, how such hierarchy is established has remained unknown so far. Here, we identify several late-acting snoRNAs that bind pre-40S particles in human cells and show that their association and function in pre-40S complexes is regulated by the RNA helicase DDX21. We map DDX21 crosslinking sites on pre-rRNAs and show their overlap with the basepairing sites of the affected snoRNAs. While DDX21 activity is required for recruitment of the late-acting snoRNAs SNORD56 and SNORD68, earlier snoRNAs are not affected by DDX21 depletion. Together, these observations provide an understanding of the timing and ordered hierarchy of snoRNP action in pre-40S maturation and reveal a novel mode of regulation of snoRNP function by an RNA helicase in human cells."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1093/nar/gku1291"],["dc.identifier.isi","000350207100052"],["dc.identifier.pmid","25477391"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11460"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38490"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.rights","CC BY-NC 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/4.0"],["dc.title","The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","209"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Kleiber, Nicole"],["dc.contributor.author","Lemus-Diaz, Nicolas"],["dc.contributor.author","Stiller, Carina"],["dc.contributor.author","Heinrichs, Marleen"],["dc.contributor.author","Mai, Mandy Mong-Quyen"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Richter-Dennerlein, Ricarda"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-02-01T10:31:09Z"],["dc.date.available","2022-02-01T10:31:09Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Modified nucleotides in tRNAs are important determinants of folding, structure and function. Here we identify METTL8 as a mitochondrial matrix protein and active RNA methyltransferase responsible for installing m 3 C 32 in the human mitochondrial (mt-)tRNA Thr and mt-tRNA Ser(UCN) . METTL8 crosslinks to the anticodon stem loop (ASL) of many mt-tRNAs in cells, raising the question of how methylation target specificity is achieved. Dissection of mt-tRNA recognition elements revealed U 34 G 35 and t 6 A 37 /(ms 2 )i 6 A 37 , present concomitantly only in the ASLs of the two substrate mt-tRNAs, as key determinants for METTL8-mediated methylation of C 32 . Several lines of evidence demonstrate the influence of U 34 , G 35 , and the m 3 C 32 and t 6 A 37 /(ms 2 )i 6 A 37 modifications in mt-tRNA Thr/Ser(UCN) on the structure of these mt-tRNAs. Although mt-tRNA Thr/Ser(UCN) lacking METTL8-mediated m 3 C 32 are efficiently aminoacylated and associate with mitochondrial ribosomes, mitochondrial translation is mildly impaired by lack of METTL8. Together these results define the cellular targets of METTL8 and shed new light on the role of m 3 C 32 within mt-tRNAs."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.doi","10.1038/s41467-021-27905-1"],["dc.identifier.pii","27905"],["dc.identifier.pmid","35017528"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98794"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/390"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/167"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-517"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","2041-1723"],["dc.relation.workinggroup","RG M. Bohnsack (Molecular Biology)"],["dc.relation.workinggroup","RG Richter-Dennerlein (Mitoribosome Assembly)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The RNA methyltransferase METTL8 installs m3C32 in mitochondrial tRNAsThr/Ser(UCN) to optimise tRNA structure and mitochondrial translation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]