Krebber, Heike

[["dc.bibliographiccitation.firstpage","1642"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","1648"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Zander, Gesa"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2020-12-10T18:15:15Z"],["dc.date.available","2020-12-10T18:15:15Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1080/15476286.2017.1345835"],["dc.identifier.eissn","1555-8584"],["dc.identifier.issn","1547-6286"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74794"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Quick or quality? How mRNA escapes nuclear quality control during stress"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","459"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.lastpage","470"],["dc.bibliographiccitation.volume","34"],["dc.contributor.author","Zander, Gesa"],["dc.contributor.author","Kramer, Wilfried"],["dc.contributor.author","Seel, Anika"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2020-12-10T14:07:16Z"],["dc.date.available","2020-12-10T14:07:16Z"],["dc.date.issued","2017"],["dc.identifier.doi","10.1002/yea.v34.11"],["dc.identifier.issn","0749-503X"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/70162"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Saccharomyces cerevisiae Gle2/Rae1 is involved in septin organization, essential for cell cycle progression"],["dc.title.alternative","Gle2 and septin formation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","gkac952"],["dc.bibliographiccitation.firstpage","11301"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Nucleic Acids Research"],["dc.bibliographiccitation.lastpage","11314"],["dc.bibliographiccitation.volume","50"],["dc.contributor.author","Klama, Sandra"],["dc.contributor.author","Hirsch, Anna G"],["dc.contributor.author","Schneider, Ulla M"],["dc.contributor.author","Zander, Gesa"],["dc.contributor.author","Seel, Anika"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2022-12-01T08:31:08Z"],["dc.date.available","2022-12-01T08:31:08Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\r\n Efficient gene expression requires properly matured mRNAs for functional transcript translation. Several factors including the guard proteins monitor maturation and act as nuclear retention factors for unprocessed pre-mRNAs. Here we show that the guard protein Npl3 monitors 5’-capping. In its absence, uncapped transcripts resist degradation, because the Rat1–Rai1 5’-end degradation factors are not efficiently recruited to these faulty transcripts. Importantly, in npl3Δ, these improperly capped transcripts escape this quality control checkpoint and leak into the cytoplasm. Our data suggest a model in which Npl3 associates with the Rai1 bound pre-mRNAs. In case the transcript was properly capped and is thus CBC (cap binding complex) bound, Rai1 dissociates from Npl3 allowing the export factor Mex67 to interact with this guard protein and support nuclear export. In case Npl3 does not detect proper capping through CBC attachment, Rai1 binding persists and Rat1 can join this 5’-complex to degrade the faulty transcript."],["dc.identifier.doi","10.1093/nar/gkac952"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118083"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-621"],["dc.relation.eissn","1362-4962"],["dc.relation.issn","0305-1048"],["dc.title","A guard protein mediated quality control mechanism monitors 5’-capping of pre-mRNAs"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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"]]