Brüning, Lukas

[["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","663"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Genome Research"],["dc.bibliographiccitation.lastpage","663"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Jungfleisch, Jennifer"],["dc.contributor.author","Nedialkova, Danny D."],["dc.contributor.author","Dotu, Ivan"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Martinez-Bosch, Neus"],["dc.contributor.author","Brüning, Lukas"],["dc.contributor.author","Raineri, Emanuele"],["dc.contributor.author","Navarro, Pilar"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Leidel, Sebastian A."],["dc.contributor.author","Díez, Juana"],["dc.date.accessioned","2022-03-01T11:46:55Z"],["dc.date.available","2022-03-01T11:46:55Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1101/gr.222133.117"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103842"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1549-5469"],["dc.relation.iserratumof","/handle/2/43637"],["dc.relation.issn","1088-9051"],["dc.title","Corrigendum: A novel translational control mechanism involving RNA structures within coding sequences"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","erratum_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","95"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Genome Research"],["dc.bibliographiccitation.lastpage","106"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Jungfleisch, Jennifer"],["dc.contributor.author","Nedialkova, Danny D."],["dc.contributor.author","Dotu, Ivan"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Martinez-Bosch, Neus"],["dc.contributor.author","Bruening, Lukas"],["dc.contributor.author","Raineri, Emanuele"],["dc.contributor.author","Navarro, Pilar"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Leide, Sebastian A."],["dc.contributor.author","Diez, Juana"],["dc.date.accessioned","2018-11-07T10:29:23Z"],["dc.date.available","2018-11-07T10:29:23Z"],["dc.date.issued","2017"],["dc.description.abstract","The impact of RNA structures in coding sequences (CDS) within mRNAs is poorly understood. Here, we identify a novel and highly conserved mechanism of translational control involving RNA structures within coding sequences and the DEAD box helicase Dhhl. Using yeast genetics and genome-wide ribosome profiling analyses, we show that this mechanism, initially derived from studies of the Brome Mosaic virus RNA genome, extends to yeast and human mRNAs highly enriched in membrane and secreted proteins. All Dhhl-dependent mRNAs, viral and cellular, share key common features. First, they contain long and highly structured CDSs, including a region located around nucleotide 70 after the translation initiation site; second, they are directly bound by Dhhl with a specific binding distribution; and third, complementary experimental approaches suggest that they are activated by Dhhl at the translation initiation step. Our results show that ribosome translocation is not the only unwinding force of CDS and uncover a novel layer of translational control that involves RNA helicases and RNA folding within CDS providing novel opportunities for regulation of membrane and secretome proteins."],["dc.identifier.doi","10.1101/gr.209015.116"],["dc.identifier.isi","000391906500009"],["dc.identifier.pmid","27821408"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/43637"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Cold Spring Harbor Lab Press, Publications Dept"],["dc.relation.haserratum","/handle/2/103842"],["dc.relation.issn","1549-5469"],["dc.relation.issn","1088-9051"],["dc.title","A novel translational control mechanism involving RNA structures within coding sequences"],["dc.type","journal_article"],["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"]]