Neumann, Bettina

[["dc.bibliographiccitation.artnumber","e0149571"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Neumann, Bettina"],["dc.contributor.author","Wu, Haijia"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T10:18:14Z"],["dc.date.available","2018-11-07T10:18:14Z"],["dc.date.issued","2016"],["dc.description.abstract","The DEAD-box RNA-helicase Dbp5/Rat8 is known for its function in nuclear mRNA export, where it displaces the export receptor Mex67 from the mRNA at the cytoplasmic side of the nuclear pore complex (NPC). Here we show that Dbp5 is also required for the nuclear export of both pre-ribosomal subunits. Yeast temperature-sensitive dbp5 mutants accumulate both ribosomal particles in their nuclei. Furthermore, Dbp5 genetically and physically interacts with known ribosomal transport factors such as Nmd3. Similar to mRNA export we show that also for ribosomal transport Dbp5 is required at the cytoplasmic side of the NPC. However, unlike its role in mRNA export, Dbp5 does not seem to undergo its ATPase cycle for this function, as ATPase-deficient dbp5 mutants that selectively inhibit mRNA export do not affect ribosomal transport. Furthermore, mutants of GLE1, the ATPase stimulating factor of Dbp5, show no major ribosomal export defects. Consequently, while Dbp5 uses its ATPase cycle to displace the export receptor Mex67 from the translocated mRNAs, Mex67 remains bound to ribosomal subunits upon transit to the cytoplasm, where it is detectable on translating ribosomes. Therefore, we propose a model, in which Dbp5 supports ribosomal transport by capturing ribosomal subunits upon their cytoplasmic appearance at the NPC, possibly by binding export factors such as Mex67. Thus, our findings reveal that although different ribonucleoparticles, mRNAs and pre-ribosomal subunits, use shared export factors, they utilize different transport mechanisms."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.1371/journal.pone.0149571"],["dc.identifier.isi","000370054100165"],["dc.identifier.pmid","26872259"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12933"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/41395"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Nuclear Export of Pre-Ribosomal Subunits Requires Dbp5, but Not as an RNA-Helicase as for mRNA Export"],["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","1"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","18"],["dc.contributor.author","Grosse, Sebastian"],["dc.contributor.author","Lu, Yen-Yun"],["dc.contributor.author","Coban, Ivo"],["dc.contributor.author","Neumann, Bettina"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2021-04-14T08:30:12Z"],["dc.date.available","2021-04-14T08:30:12Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1080/15476286.2020.1851506"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/83144"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.title","Nuclear SR-protein mediated mRNA quality control is continued in cytoplasmic nonsense-mediated decay"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2199"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","2218"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Opitz, Nadine"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Hofer-Pretz, Verena"],["dc.contributor.author","Neumann, Bettina"],["dc.contributor.author","Krebber, Heike"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Valerius, Oliver"],["dc.date.accessioned","2020-12-10T18:12:59Z"],["dc.date.available","2020-12-10T18:12:59Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1074/mcp.M116.066654"],["dc.identifier.eissn","1535-9484"],["dc.identifier.issn","1535-9476"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74552"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Capturing the Asc1p/ R eceptor for A ctivated C K inase 1 (RACK1) Microenvironment at the Head Region of the 40S Ribosome with Quantitative BioID in Yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4798"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","4813"],["dc.bibliographiccitation.volume","47"],["dc.contributor.author","Beissel, Christian"],["dc.contributor.author","Neumann, Bettina"],["dc.contributor.author","Uhse, Simon"],["dc.contributor.author","Hampe, Irene"],["dc.contributor.author","Karki, Prajwal"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2019-07-25T10:31:21Z"],["dc.date.available","2019-07-25T10:31:21Z"],["dc.date.issued","2019"],["dc.description.abstract","Translation termination requires eRF1 and eRF3 for polypeptide- and tRNA-release on stop codons. Additionally, Dbp5/DDX19 and Rli1/ABCE1 are required; however, their function in this process is currently unknown. Using a combination of in vivo and in vitro experiments, we show that they regulate a stepwise assembly of the termination complex. Rli1 and eRF3-GDP associate with the ribosome first. Subsequently, Dbp5-ATP delivers eRF1 to the stop codon and in this way prevents a premature access of eRF3. Dbp5 dissociates upon placing eRF1 through ATP-hydrolysis. This in turn enables eRF1 to contact eRF3, as the binding of Dbp5 and eRF3 to eRF1 is mutually exclusive. Defects in the Dbp5-guided eRF1 delivery lead to premature contact and premature dissociation of eRF1 and eRF3 from the ribosome and to subsequent stop codon readthrough. Thus, the stepwise Dbp5-controlled termination complex assembly is essential for regular translation termination events. Our data furthermore suggest a possible role of Dbp5/DDX19 in alternative translation termination events, such as during stress response or in developmental processes, which classifies the helicase as a potential drug target for nonsense suppression therapy to treat cancer and neurodegenerative diseases."],["dc.identifier.doi","10.1093/nar/gkz177"],["dc.identifier.pmid","30873535"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16303"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62049"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.relation.issn","1362-4962"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Translation termination depends on the sequential ribosomal entry of eRF1 and eRF3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]