Bohnsack, Markus T.

[["dc.bibliographiccitation.firstpage","1115"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","1130"],["dc.bibliographiccitation.volume","1803"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schleiff, Enrico"],["dc.date.accessioned","2022-03-01T11:44:46Z"],["dc.date.available","2022-03-01T11:44:46Z"],["dc.date.issued","2010"],["dc.identifier.doi","10.1016/j.bbamcr.2010.06.005"],["dc.identifier.pii","S0167488910001758"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103114"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0167-4889"],["dc.title","The evolution of protein targeting and translocation systems"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["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","2004"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","2014"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Warda, Ahmed S"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Lenz, Christof"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Sloan, Katherine E"],["dc.contributor.author","Bohnsack, Markus T"],["dc.date.accessioned","2020-12-10T18:42:38Z"],["dc.date.available","2020-12-10T18:42:38Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.15252/embr.201744940"],["dc.identifier.eissn","1469-3178"],["dc.identifier.issn","1469-221X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78032"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Human METTL16 is a N 6 ‐methyladenosine (m 6 A) methyltransferase that targets pre‐mRNAs and various non‐coding RNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","629"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","639"],["dc.bibliographiccitation.volume","36"],["dc.contributor.author","Leulliot, N."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Graille, M."],["dc.contributor.author","Tollervey, D."],["dc.contributor.author","Van Tilbeurgh, H."],["dc.date.accessioned","2022-03-01T11:46:48Z"],["dc.date.available","2022-03-01T11:46:48Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1093/nar/gkm1074"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103800"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["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","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","1043"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.bibliographiccitation.lastpage","1056"],["dc.bibliographiccitation.volume","80"],["dc.contributor.author","Weis, Benjamin L."],["dc.contributor.author","Missbach, Sandra"],["dc.contributor.author","Marzi, Julian"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Schleiff, Enrico"],["dc.date.accessioned","2018-11-07T09:32:01Z"],["dc.date.available","2018-11-07T09:32:01Z"],["dc.date.issued","2014"],["dc.description.abstract","Ribosome biogenesis involves a large ensemble of trans-acting factors, which catalyse rRNA processing, ribosomal protein association and ribosomal subunit assembly. The circularly permuted GTPase Lsg1 is such a ribosome biogenesis factor, which is involved in maturation of the pre-60S ribosomal subunit in yeast. We identified two orthologues of Lsg1 in Arabidopsis thaliana. Both proteins differ in their C-terminus, which is highly charged in atLSG1-2 but missing in atLSG1-1. This C-terminus of atLSG1-2 contains a functional nuclear localization signal in a part of the protein that also targets atLSG1-2 to the nucleolus. Furthermore, only atLSG1-2 is physically associated with ribosomes suggesting its function in ribosome biogenesis. Homozygous T-DNA insertion lines are viable for both LSG1 orthologues. In plants lacking atLSG1-2 18S rRNA precursors accumulate and a 20S pre-rRNA is detected, while the amount of pre-rRNAs that lead to the 25S and 5.8S rRNA is not changed. Thus, our results suggest that pre-60S subunit maturation is important for the final steps of pre-40S maturation in plants. In addition, the lsg1-2 mutants show severe developmental defects, including triple cotyledons and upward curled leaves, which link ribosome biogenesis to early plant and leaf development."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB902]"],["dc.identifier.doi","10.1111/tpj.12703"],["dc.identifier.isi","000346280700009"],["dc.identifier.pmid","25319368"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31653"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1365-313X"],["dc.relation.issn","0960-7412"],["dc.title","The 60S associated ribosome biogenesis factor LSG1-2 is required for 40S maturation in Arabidopsis thaliana"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1532"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1543"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Haag, Sara"],["dc.contributor.author","Warda, Ahmed S."],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Guennigmann, Manuel A."],["dc.contributor.author","Hoebartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:52:51Z"],["dc.date.available","2018-11-07T09:52:51Z"],["dc.date.issued","2015"],["dc.description.abstract","Many cellular RNAs require modification of specific residues for their biogenesis, structure, and function. 5-methylcytosine (m(5)C) is a common chemical modification in DNA and RNA but in contrast to the DNA modifying enzymes, only little is known about the methyltransferases that establish m(5)C modifications in RNA. The putative RNA methyltransferase NSUN6 belongs to the family of Nol1/Nop2/SUN domain (NSUN) proteins, but so far its cellular function has remained unknown. To reveal the target spectrum of human NSUN6, we applied UV crosslinking and analysis of cDNA (CRAC) as well as chemical crosslinking with 5-azacytidine. We found that human NSUN6 is associated with tRNAs and acts as a tRNA methyltransferase. Furthermore, we uncovered tRNACys and tRNAThr as RNA substrates of NSUN6 and identified the cytosine C72 at the 3' end of the tRNA acceptor stem as the target nucleoside. Interestingly, target recognition in vitro depends on the presence of the 3'-CCA tail. Together with the finding that NSUN6 localizes to the cytoplasm and largely colocalizes with marker proteins for the Golgi apparatus and pericentriolar matrix, our data suggest that NSUN6 modifies tRNAs in a late step in their biogenesis."],["dc.identifier.doi","10.1261/rna.051524.115"],["dc.identifier.isi","000359996100002"],["dc.identifier.pmid","26160102"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36208"],["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","NSUN6 is a human RNA methyltransferase that catalyzes formation of m(5)C72 in specific tRNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","397"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Wiley Interdisciplinary Reviews: RNA"],["dc.bibliographiccitation.lastpage","414"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Watkins, Nicholas J."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2022-03-01T11:46:50Z"],["dc.date.available","2022-03-01T11:46:50Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1002/wrna.117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103815"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","1757-7004"],["dc.title","The box C/D and H/ACA snoRNPs: key players in the modification, processing and the dynamic folding of ribosomal RNA"],["dc.title.alternative","Box C/D and H/ACA snoRNPs"],["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"]]