Krebber, Heike

[["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","4811"],["dc.bibliographiccitation.issue","24"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","4823"],["dc.bibliographiccitation.volume","33"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Gross, Thomas"],["dc.contributor.author","Henker, Lysann"],["dc.contributor.author","Hinz, Frederik"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T09:17:14Z"],["dc.date.available","2018-11-07T09:17:14Z"],["dc.date.issued","2013"],["dc.description.abstract","The yeast shuttling serine/arginine-rich protein Npl3 is required for the export of mRNAs and pre-60S ribosomal subunits from the nucleus to the cytoplasm. Here, we report a novel function of Npl3 in translation initiation. A mutation in its C terminus that prevents its dimerization (npl3 Delta 100) is lethal to cells and leads to translational defects, as shown by [S-35] methionine incorporation assays and a hypersensitivity to the translational inhibitor cycloheximide. Moreover, this Npl3 mutant shows halfmers in polysomal profiles that are indicative of defects in monosome formation. Strikingly, the loss of the ability of Npl3 to dimerize does not affect mRNA and pre-60S export. In fact, the mRNA and rRNA binding capacities of npl3 Delta 100 and wild-type Npl3 are similar. Intriguingly, overexpression of the dimerization domain of Npl3 disturbs dimer formation and results in a dominant-negative effect, reflected in growth defects and a halfmer formation phenotype. In addition, we found specific genetic interactions with the ribosomal subunit joining factors Rpl10 and eukaryotic translation initiation factor 5B/Fun12 and detected a substantially decreased binding of npl3 Delta 100 to the Rpl10-containing complex. These findings indicate an essential novel function for Npl3 in the cytoplasm, which supports monosome formation for translation initiation."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.1128/MCB.00873-13"],["dc.identifier.isi","000327544200004"],["dc.identifier.pmid","24100011"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28116"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","1098-5549"],["dc.relation.issn","0270-7306"],["dc.title","Monosome Formation during Translation Initiation Requires the Serine/Arginine-Rich Protein Npl3"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","593"],["dc.bibliographiccitation.issue","7634"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","+"],["dc.bibliographiccitation.volume","540"],["dc.contributor.author","Zander, Gesa"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Bender, Lysann"],["dc.contributor.author","Becker, Daniel"],["dc.contributor.author","Lingner, Thomas"],["dc.contributor.author","Salinas, Gabriela"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T10:04:24Z"],["dc.date.available","2018-11-07T10:04:24Z"],["dc.date.issued","2016"],["dc.description.abstract","Cells grow well only in a narrow range of physiological conditions. Surviving extreme conditions requires the instantaneous expression of chaperones that help to overcome stressful situations. To ensure the preferential synthesis of these heat-shock proteins, cells inhibit transcription, pre-mRNA processing and nuclear export of non-heat-shock transcripts, while stress-specific mRNAs are exclusively exported and translated1. How cells manage the selective retention of regular transcripts and the simultaneous rapid export of heat-shock mRNAs is largely unknown. In Saccharomyces cerevisiae, the shuttling RNA adaptor proteins Npl3, Gbp2, Hrb1 and Nab2 are loaded co-transcriptionally onto growing pre-mRNAs. For nuclear export, they recruit the export-receptor heterodimer Mex67-Mtr2 (TAP-p15 in humans)(2). Here we show that cellular stress induces the dissociation of Mex67 and its adaptor proteins from regular mRNAs to prevent general mRNA export. At the same time, heat-shock mRNAs are rapidly exported in association with Mex67, without the need for adapters. The immediate co-transcriptional loading of Mex67 onto heat-shock mRNAs involves Hsf1, a heat-shock transcription factor that binds to heat-shock-promoter elements in stress-responsive genes. An important difference between the export modes is that adaptor-protein-bound mRNAs undergo quality control, whereas stress-specific transcripts do not. In fact, regular mRNAs are converted into uncontrolled stress-responsive transcripts if expressed under the control of a heat-shock promoter, suggesting that whether an mRNA undergoes quality control is encrypted therein. Under normal conditions, Mex67 adaptor proteins are recruited for RNA surveillance, with only quality-controlled mRNAs allowed to associate with Mex67 and leave the nucleus. Thus, at the cost of error-free mRNA formation, heat-shock mRNAs are exported and translated without delay, allowing cells to survive extreme situations."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft; [SFB860]"],["dc.identifier.doi","10.1038/nature20572"],["dc.identifier.isi","000391190500054"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38688"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1476-4687"],["dc.relation.issn","0028-0836"],["dc.title","mRNA quality control is bypassed for immediate export of stress-responsive transcripts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Gross, Thomas"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T09:20:12Z"],["dc.date.available","2018-11-07T09:20:12Z"],["dc.date.issued","2013"],["dc.format.extent","98"],["dc.identifier.isi","000327927400144"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28828"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th International Conference on Yeast Genetics and Molecular Biology"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","The mRNA export factor Npl3 mediates the nuclear export of large ribosomal subunits"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1024"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","EMBO Reports"],["dc.bibliographiccitation.lastpage","1031"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Gross, Thomas"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T08:51:15Z"],["dc.date.available","2018-11-07T08:51:15Z"],["dc.date.issued","2011"],["dc.description.abstract","The nuclear export of large ribonucleoparticles is complex and requires specific transport factors. Messenger RNAs are exported through the RNA-binding protein Npl3 and the interacting export receptor Mex67. Export of large ribosomal subunits also requires Mex67; however, in this case, Mex67 binds directly to the 5S ribosomal RNA (rRNA) and does not require the Npl3 adaptor. Here, we have discovered a new function of Npl3 in mediating the export of pre-60S ribosomal subunit independently of Mex67. Npl3 interacts with the 25S rRNA, ribosomal and ribosome-associated proteins, as well as with the nuclear pore complex. Mutations in NPL3 lead to export defects of the large subunit and genetic interactions with other pre-60S export factors."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft; [SFB593]; [SFB860]"],["dc.identifier.doi","10.1038/embor.2011.155"],["dc.identifier.isi","000295459700013"],["dc.identifier.pmid","21852791"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21888"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1469-221X"],["dc.title","The mRNA export factor Npl3 mediates the nuclear export of large ribosomal subunits"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","3123"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","5"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Wu, Haijia"],["dc.contributor.author","Schneider, Ulla-Maria"],["dc.contributor.author","Meyer, Katja"],["dc.contributor.author","Jung, Klaus"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T09:46:38Z"],["dc.date.available","2018-11-07T09:46:38Z"],["dc.date.issued","2014"],["dc.description.abstract","Eukaryotic cells have to prevent the export of unspliced pre-mRNAs until intron removal is completed to avoid the expression of aberrant and potentially harmful proteins. Only mature mRNAs associate with the export receptor Mex67/TAP and enter the cytoplasm. Here we show that the two shuttling serine/arginine (SR)-proteins Gbp2 and Hrb1 are key surveillance factors for the selective export of spliced mRNAs in yeast. Their absence leads to the significant leakage of unspliced pre-mRNAs into the cytoplasm. They bind to pre-mRNAs and the spliceosome during splicing, where they are necessary for the surveillance of splicing and the stable binding of the TRAMP complex to spliceosome-bound transcripts. Faulty transcripts are marked for their degradation at the nuclear exosome. On correct mRNAs the SR proteins recruit Mex67 upon completion of splicing to allow a quality controlled nuclear export. Altogether, these data identify a role for shuttling SR proteins in mRNA surveillance and nuclear mRNA quality control."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft; [SFB 860]"],["dc.identifier.doi","10.1038/ncomms4123"],["dc.identifier.isi","000331084400032"],["dc.identifier.pmid","24452287"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34922"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.title","Quality control of spliced mRNAs requires the shuttling SR proteins Gbp2 and Hrb1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Hackmann, Alexandra"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T09:20:10Z"],["dc.date.available","2018-11-07T09:20:10Z"],["dc.date.issued","2013"],["dc.format.extent","42"],["dc.identifier.isi","000327927400039"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28819"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th International Conference on Yeast Genetics and Molecular Biology"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","Cellular functions of the SR-proteins in S. cerevisiae"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]