Krebber, Heike

[["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","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.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.firstpage","548"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","550"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2018-11-07T08:40:10Z"],["dc.date.available","2018-11-07T08:40:10Z"],["dc.date.issued","2010"],["dc.description.abstract","In eukaryotes, translation termination requires two eukaryotic release factors, eRF1 and eRF3. eRF1 is required for recognition of the stop codon and eRF3 supports the polypeptide chain release in a GTP dependent manner. Recently, several new players in translation termination have been identified. The DEAD-box RNA helicase Dbp5 has been shown to support eRF1 in stop codon recognition, possibly by proper placement of the release factor on the termination codon. Upon its dissociation from eRF1, Dbp5 allows the entry of the second termination factor eRF3 into the complex. Further, the Dbp5 interacting protein Gle1 and its co-factor inositol hexakisphosphate ( IP 6) have been shown to participate in the termination process. Dbp5 and Gle1 are well known for their function in mRNA export from the nucleus to the cytoplasm. Most interestingly, also the ATP binding cassette ( ABC) protein Rli1, which requires the mitochondrial and cytosolic Fe/ S protein biogenesis machineries for its assembly, has recently been shown to function in translation termination and recycling of the ribosomes. Rli1 physically and genetically interacts with both, eRF1 and eRF3. Together, all of these novel termination factors modulate in association with the release factors more accurate stop codon recognition and these findings broaden our knowledge about the final steps in translation."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.identifier.isi","000288456500007"],["dc.identifier.pmid","21081843"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19163"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Landes Bioscience"],["dc.relation.issn","1547-6286"],["dc.title","Translation termination New factors and insights"],["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"]]

[["dc.bibliographiccitation.firstpage","214"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","EMBO reports"],["dc.bibliographiccitation.lastpage","219"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Khoshnevis, Sohail"],["dc.contributor.author","Gross, Thomas"],["dc.contributor.author","Rotte, Carmen"],["dc.contributor.author","Baierlein, Claudia"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2017-09-07T11:46:09Z"],["dc.date.available","2017-09-07T11:46:09Z"],["dc.date.issued","2010"],["dc.description.abstract","The iron-sulphur (Fe-S)-containing RNase L inhibitor (Rli1) is involved in ribosomal subunit maturation, transport of both ribosomal subunits to the cytoplasm, and translation initiation through interaction with the eukaryotic initiation factor 3 (eIF3) complex. Here, we present a new function for Rli1 in translation termination. Through co-immunoprecipitation experiments, we show that Rli1 interacts physically with the translation termination factors eukaryotic release factor 1 (eRF1)/Sup45 and eRF3/Sup35 in Saccharomyces cerevisiae. Genetic interactions were uncovered between a strain depleted for Rli1 and sup35-21 or sup45-2. Furthermore, we show that downregulation of RLI1 expression leads to defects in the recognition of a stop codon, as seen in mutants of other termination factors. By contrast, RLI1 overexpression partly suppresses the read-through defects in sup45-2. Interestingly, we find that although the Fe-S cluster is not required for the interaction of Rli1 with eRF1 or its other interacting partner, Hcr1, from the initiation complex eIF3, it is required for its activity in translation termination; an Fe-S cluster mutant of RLI1 cannot suppress the read-through defects of sup45-2."],["dc.identifier.doi","10.1038/embor.2009.272"],["dc.identifier.gro","3142957"],["dc.identifier.isi","000275056700020"],["dc.identifier.pmid","20062004"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/418"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","1469-221X"],["dc.title","The iron-sulphur protein RNase L inhibitor functions in translation termination"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]