Krebber, Heike

[["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","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.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.artnumber","22174"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Hirsch, Anna Greta"],["dc.contributor.author","Becker, Daniel"],["dc.contributor.author","Lamping, Jan-Philipp"],["dc.contributor.author","Krebber, Heike"],["dc.date.accessioned","2021-12-01T09:23:04Z"],["dc.date.available","2021-12-01T09:23:04Z"],["dc.date.issued","2021"],["dc.description.abstract","Telomerases elongate the ends of chromosomes required for cell immortality through their reverse transcriptase activity. By using the model organism Saccharomyces cerevisiae we defined the order in which the holoenzyme matures. First, a longer precursor of the telomerase RNA, TLC1 is transcribed and exported into the cytoplasm, where it associates with the protecting Sm-ring, the Est and the Pop proteins. This partly matured telomerase is re-imported into the nucleus via Mtr10 and a novel TLC1 -import factor, the karyopherin Cse1. Remarkably, while mutations in all known transport factors result in short telomere ends, mutation in CSE1 leads to the amplification of Y′ elements in the terminal chromosome regions and thus elongated telomere ends. Cse1 does not only support TLC1 import, but also the Sm-ring stabilization on the RNA enableling Mtr10 contact and nuclear import. Thus, Sm-ring formation and import factor contact resembles a quality control step in the maturation process of the telomerase. The re-imported immature TLC1 is finally trimmed into the 1158 nucleotides long mature form via the nuclear exosome. TMG-capping of TLC1 finalizes maturation, leading to mature telomerase."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41598-021-01599-3"],["dc.identifier.pii","1599"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94552"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.title","Unraveling the stepwise maturation of the yeast telomerase including a Cse1 and Mtr10 mediated quality control checkpoint"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]