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","3199"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","3214.e3"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Becker, Daniel"],["dc.contributor.author","Hirsch, Anna Greta"],["dc.contributor.author","Bender, Lysann"],["dc.contributor.author","Lingner, Thomas"],["dc.contributor.author","Salinas, Gabriela"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2020-12-10T14:23:02Z"],["dc.date.available","2020-12-10T14:23:02Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.celrep.2019.05.031"],["dc.identifier.issn","2211-1247"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16442"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71808"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Nuclear Pre-snRNA Export Is an Essential Quality Assurance Mechanism for Functional Spliceosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["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.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.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","1630"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","1638"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Wu, Haijia"],["dc.contributor.author","Becker, Daniel"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T09:35:03Z"],["dc.date.available","2018-11-07T09:35:03Z"],["dc.date.issued","2014"],["dc.description.abstract","Telomerases protect the ends of linear chromosomes from shortening. They are composed of an RNA (TLC1 in S. cerevisiae) and several proteins. TLC1 undergoes several maturation steps before it is exported into the cytoplasm to recruit the Est proteins for complete assembly. The mature telomerase is subsequently reimported into the nucleus, where it fulfills its function on telomeres. Here, we show that TLC1 export into the cytoplasm requires not only the Ran GTPase-dependent karyopherin Crm1/Xpo1 but also the mRNA export machinery. mRNA export factor mutants accumulate mature and export-competent TLC1 RNAs in their nuclei. Moreover, TLC1 physically interacts with the mRNA transport factors Mex67 and Dbp5/Rat8. Most importantly, we show that the nuclear export of TLC1 is an essential step for the formation of the functional RNA containing enzyme, because blocking TLC1 export in the mex67-5 xpo1-1 double mutant prevents its cytoplasmic maturation and leads to telomere shortening."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (DFG); [SFB 860]"],["dc.identifier.doi","10.1016/j.celrep.2014.08.021"],["dc.identifier.isi","000343867400004"],["dc.identifier.pmid","25220466"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11359"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32308"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","Telomerase RNA TLC1 Shuttling to the Cytoplasm Requires mRNA Export Factors and Is Important for Telomere Maintenance"],["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.artnumber","UNSP e63745"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Kari, Vijayalakshmi"],["dc.contributor.author","Karpiuk, Oleksandra"],["dc.contributor.author","Tieg, Bettina"],["dc.contributor.author","Kriegs, Malte"],["dc.contributor.author","Dikomey, Ekkehard"],["dc.contributor.author","Krebber, Heike"],["dc.contributor.author","Begus-Nahrmann, Yvonne"],["dc.contributor.author","Johnsen, Steven A."],["dc.date.accessioned","2018-11-07T09:24:36Z"],["dc.date.available","2018-11-07T09:24:36Z"],["dc.date.issued","2013"],["dc.description.abstract","Unlike other metazoan mRNAs, replication-dependent histone gene transcripts are not polyadenylated but instead have a conserved stem-loop structure at their 39 end. Our previous work has shown that under certain conditions replication-dependent histone genes can produce alternative transcripts that are polyadenylated at the 39 end and, in some cases, spliced. A number of microarray studies examining the expression of polyadenylated mRNAs identified changes in the levels of histone transcripts e. g. during differentiation and tumorigenesis. However, it remains unknown which histone genes produce polyadenylated transcripts and which conditions regulate this process. In the present study we examined the expression and polyadenylation of the human histone H2B gene complement in various cell lines. We demonstrate that H2B genes display a distinct expression pattern that is varies between different cell lines. Further we show that the fraction of polyadenylated HIST1H2BD and HIST1H2AC transcripts is increased during differentiation of human mesenchymal stem cells (hMSCs) and human fetal osteoblast (hFOB 1.19). Furthermore, we observed an increased fraction of polyadenylated transcripts produced from the histone genes in cells following ionizing radiation. Finally, we show that polyadenylated transcripts are transported to the cytoplasm and found on polyribosomes. Thus, we propose that the production of polyadenylated histone mRNAs from replication-dependent histone genes is a regulated process induced under specific cellular circumstances."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.identifier.doi","10.1371/journal.pone.0063745"],["dc.identifier.isi","000320362700053"],["dc.identifier.pmid","23717473"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9111"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29865"],["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-NC-ND 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/3.0"],["dc.title","A Subset of Histone H2B Genes Produces Polyadenylated mRNAs under a Variety of Cellular Conditions"],["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"]]