Bohnsack, Markus T.

[["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.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.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Jia, Junqiao"],["dc.contributor.author","Absmeier, Eva"],["dc.contributor.author","Holton, Nicole"],["dc.contributor.author","Pietrzyk-Brzezinska, Agnieszka J."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Wahl, Markus C."],["dc.date.accessioned","2021-04-14T08:31:48Z"],["dc.date.available","2021-04-14T08:31:48Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1038/s41467-020-19221-x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83718"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2041-1723"],["dc.title","The interaction of DNA repair factors ASCC2 and ASCC3 is affected by somatic cancer mutations"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","209"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","210"],["dc.bibliographiccitation.volume","282"],["dc.contributor.author","Heininger, A. U."],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Andreou, Alexandra-Zoi"],["dc.contributor.author","Boon, K.-L."],["dc.contributor.author","Prior, M."],["dc.contributor.author","Schmidt, B."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2018-11-07T09:54:51Z"],["dc.date.available","2018-11-07T09:54:51Z"],["dc.date.issued","2015"],["dc.identifier.isi","000362570603174"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36625"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.eventlocation","Berlin, GERMANY"],["dc.relation.issn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Sequestering and protein cofactor competition regulate a multifunctional RNA helicase in different pathways"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","12"],["dc.contributor.author","Choudhury, Priyanka"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2021-04-14T08:31:39Z"],["dc.date.available","2021-04-14T08:31:39Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1080/15476286.2020.1829366"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83670"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.title","The DExD box ATPase DDX55 is recruited to domain IV of the 28S ribosomal RNA by its C-terminal region"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1339"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","RNA"],["dc.bibliographiccitation.lastpage","1350"],["dc.bibliographiccitation.volume","24"],["dc.contributor.author","Kretschmer, Jens"],["dc.contributor.author","Rao, Harita"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Höbartner, Claudia"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:41:55Z"],["dc.date.available","2020-12-10T18:41:55Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1261/rna.064238.117"],["dc.identifier.eissn","1469-9001"],["dc.identifier.issn","1355-8382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77730"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The m 6 A reader protein YTHDC2 interacts with the small ribosomal subunit and the 5′–3′ exoribonuclease XRN1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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","539"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","553"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Davila Gallesio, Jimena"],["dc.contributor.author","Hackert, Philipp"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2020-12-10T18:15:16Z"],["dc.date.available","2020-12-10T18:15:16Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1080/15476286.2020.1716540"],["dc.identifier.eissn","1555-8584"],["dc.identifier.issn","1547-6286"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74799"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Sgd1 is an MIF4G domain-containing cofactor of the RNA helicase Fal1 and associates with the 5’ domain of the 18S rRNA sequence"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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"]]

[["dc.bibliographiccitation.firstpage","320"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Heininger, Annika U."],["dc.contributor.author","Hackert, Phillip"],["dc.contributor.author","Andreou, Alexandra Z."],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.identifier.doi","10.1080/15476286.2016.1142038"],["dc.identifier.gro","3141714"],["dc.identifier.isi","000372909600008"],["dc.identifier.pmid","26821976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/258"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]