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","499"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","519"],["dc.bibliographiccitation.volume","104"],["dc.contributor.author","Ariyachet, Chaiyaboot"],["dc.contributor.author","Beissel, Christian"],["dc.contributor.author","Li, Xiang"],["dc.contributor.author","Lorrey, Selena"],["dc.contributor.author","Mackenzie, Olivia"],["dc.contributor.author","Martin, Patrick M."],["dc.contributor.author","O'Brien, Katharine"],["dc.contributor.author","Pholcharee, Tossapol"],["dc.contributor.author","Sim, Sue"],["dc.contributor.author","Krebber, Heike"],["dc.contributor.author","McBride, Anne E."],["dc.date.accessioned","2018-11-07T10:24:44Z"],["dc.date.available","2018-11-07T10:24:44Z"],["dc.date.issued","2017"],["dc.description.abstract","The morphological transition of the opportunistic fungal pathogen Candida albicans from budding to hyphal growth has been implicated in its ability to cause disease in animal models. Absence of styled-content NA-binding protein Slr1 slows hyphal formation and decreases virulence in a systemic candidiasis model, suggesting a role for post-transcriptional regulation in these processes. SR (serine-arginine)-rich proteins influence multiple steps in mRNA metabolism and their localization and function are frequently controlled by modification. We now demonstrate that Slr1 binds to polyadenylated RNA and that its intracellular localization is modulated by phosphorylation and methylation. Wildtype Slr1-GFP is predominantly nuclear, but also co-fractionates with translating ribosomes. The non-phosphorylatable slr1-6SA-GFP protein, in which six serines in SR/RS clusters are substituted with alanines, primarily localizes to the cytoplasm in budding cells. Intriguingly, hyphal cells display a slr1-6SA-GFP focus at the tip near the Spitzenkorper, a vesicular structure involved in molecular trafficking to the tip. The presence of slr1-6SA-GFP hyphal tip foci is reduced in the absence of the mRNA-transport protein She3, suggesting that unphosphorylated Slr1 associates with mRNA-protein complexes transported to the tip. The impact of SLR1 deletion on hyphal formation and function thus may be partially due to a role in hyphal mRNA transport."],["dc.identifier.doi","10.1111/mmi.13643"],["dc.identifier.isi","000399665400010"],["dc.identifier.pmid","28187496"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42714"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley"],["dc.relation.issn","1365-2958"],["dc.relation.issn","0950-382X"],["dc.title","Post-translational modification directs nuclear and hyphal tip localization of Candida albicans mRNA-binding protein Slr1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","534"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Journal of Bacteriology"],["dc.bibliographiccitation.lastpage","544"],["dc.bibliographiccitation.volume","195"],["dc.contributor.author","Lehnik-Habrink, Martin"],["dc.contributor.author","Rempeters, Leonie"],["dc.contributor.author","Kovacs, Akos T."],["dc.contributor.author","Wrede, Christoph"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Krebber, Heike"],["dc.contributor.author","Kuipers, Oscar P."],["dc.contributor.author","Stuelke, Joerg"],["dc.date.accessioned","2018-11-07T09:28:21Z"],["dc.date.available","2018-11-07T09:28:21Z"],["dc.date.issued","2013"],["dc.description.abstract","DEAD-box RNA helicases play important roles in remodeling RNA molecules and in facilitating a variety of RNA-protein interactions that are key to many essential cellular processes. In spite of the importance of RNA, our knowledge about RNA helicases is limited. In this study, we investigated the role of the four DEAD-box RNA helicases in the Gram-positive model organism Bacillus subtilis. A strain deleted of all RNA helicases is able to grow at 37 degrees C but not at lower temperatures. The deletion of cshA, cshB, or yfmL in particular leads to cold-sensitive phenotypes. Moreover, these mutant strains exhibit unique defects in ribosome biogenesis, suggesting distinct functions for the individual enzymes in this process. Based on protein accumulation, severity of the cold-sensitive phenotype, and the interaction with components of the RNA degradosome, CshA is the major RNA helicase of B. subtilis. To unravel the functions of CshA in addition to ribosome biogenesis, we conducted microarray analysis and identified the ysbAB and frlBONMD mRNAs as targets that are strongly affected by the deletion of the cshA gene. Our findings suggest that the different helicases make distinct contributions to the physiology of B. subtilis. Ribosome biogenesis and RNA degradation are two of their major tasks in B. subtilis."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft [SFB860]"],["dc.identifier.doi","10.1128/JB.01475-12"],["dc.identifier.isi","000316960800015"],["dc.identifier.pmid","23175651"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30755"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0021-9193"],["dc.title","DEAD-Box RNA Helicases in Bacillus subtilis Have Multiple Functions and Act Independently from Each Other"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["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.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.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"]]

[["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.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"]]