Irniger, Stefan

[["dc.bibliographiccitation.firstpage","31"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","43"],["dc.bibliographiccitation.volume","378"],["dc.contributor.author","Sari, Fatih"],["dc.contributor.author","Heinrich, Melanie"],["dc.contributor.author","Meyeri, Wibke"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, Stefan"],["dc.date.accessioned","2018-11-07T11:16:02Z"],["dc.date.available","2018-11-07T11:16:02Z"],["dc.date.issued","2008"],["dc.description.abstract","The cyclin-dependent kinase CdkI and the related kinase Ime2 act in concert to trigger progression of the meiotic cell cycle in the yeast Saccharomyces cerevisiae. These kinases share several functions and substrates during meiosis, but their regulation seems to be clearly different. In contrast to Cdk1, no cyclin seems to be involved in the regulation of Ime2 activity. Ime2 is a highly unstable protein, and we aimed to elucidate the relevance of Ime2 instability. We first determined the sequence elements required for Ime2 instability by constructing a set of deletions in the IME2 gene. None of the small deletions in Ime2 affected its instability but deletion of a 241 amino acid C-terminal region resulted in a highly stabilized protein. Thus, the C-terminal domain of Ime2 is important for mediating protein instability. The stabilized, truncated Ime2 protein is highly active in vivo. Replacement of the IME2 gene with the truncated IME2 Delta C241 in diploid strains did not interfere with meiotic nuclear divisions, but caused abnormalities in spore formation, as manifested by the appearance of many asci with a reduced spore number such as triads and dyads. The truncated Ime2 caused a reduction of spore number in a dominant manner. We conclude that downregulation of Ime2 kinase activity mediated by the C-terminal domain is required for the efficient production of normal four-spore asci. Our data suggest a role for Ime2 in spore number control in S. cerevisiae."],["dc.identifier.doi","10.1016/j.jmb.2008.02.001"],["dc.identifier.isi","000255368200004"],["dc.identifier.pmid","18339400"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/54501"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd- Elsevier Science Ltd"],["dc.relation.issn","1089-8638"],["dc.relation.issn","0022-2836"],["dc.title","The C-terminal region of the meiosis-specific protein kinase Ime2 mediates protein instability and is required for normal spore formation in budding yeast"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","327"],["dc.bibliographiccitation.issue","5-6"],["dc.bibliographiccitation.journal","Current Genetics"],["dc.bibliographiccitation.lastpage","334"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Strittmatter, Axel W."],["dc.contributor.author","Irniger, S."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T08:54:27Z"],["dc.date.available","2018-11-07T08:54:27Z"],["dc.date.issued","2001"],["dc.description.abstract","The jlbA (jun-like bZIP) gene of Aspergillus nidulans was isolated. The deduced amino acid motif of the C-terminal region of jlbA encodes a putative DNA-binding site composed of a basic amino acid domain and an adjacent leucine zipper motif. This region shares highest similarities to the C-terminal DNA-binding domain and the basic zipper (bZIP)-motifs of transcription factors like CPCA from A. niger, Gcn4p from Saccharomyces cerevisiae, human JUNB and c-JUN. The putative jlbA protein contains a PEST-rich region (an instability region rich in the an-Lino acids proline, glutamic acid, serine and threonine) described to be implicated in protein stability. The jlbA mRNA formation is elevated up to 40-fold upon amino acid starvation induced by the addition of the false feedback inhibitor 3-amino-1,2,4-triazole. This induction is partially dependent and partially independent on the presence of the transcription factor CPCA. Therefore jlbA is a novel,gene of A. nidulans which is transcriptionally activated by amino acid starvation conditions."],["dc.identifier.isi","000170521300008"],["dc.identifier.pmid","11525406"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22676"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0172-8083"],["dc.title","Induction of jlbA mRNA synthesis for a putative bZIP protein of Aspergillus nidulans by amino acid starvation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","27567"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","27579"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Petroi, Doris"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Taheri-Talesh, Naimeh"],["dc.contributor.author","Irniger, Stefan"],["dc.contributor.author","Shahpasandzadeh, Hedieh"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T08:45:30Z"],["dc.date.available","2018-09-28T08:45:30Z"],["dc.date.issued","2012"],["dc.description.abstract","Parkinson disease is the second most common neurodegenerative disease. The molecular hallmark is the accumulation of proteinaceous inclusions termed Lewy bodies containing misfolded and aggregated α-synuclein. The molecular mechanism of clearance of α-synuclein aggregates was addressed using the bakers' yeast Saccharomyces cerevisiae as the model. Overexpression of wild type α-synuclein or the genetic variant A53T integrated into one genomic locus resulted in a gene copy-dependent manner in cytoplasmic proteinaceous inclusions reminiscent of the pathogenesis of the disease. In contrast, overexpression of the genetic variant A30P resulted only in transient aggregation, whereas the designer mutant A30P/A36P/A76P neither caused aggregation nor impaired yeast growth. The α-synuclein accumulation can be cleared after promoter shut-off by a combination of autophagy and vacuolar protein degradation. Whereas the proteasomal inhibitor MG-132 did not significantly inhibit aggregate clearance, treatment with phenylmethylsulfonyl fluoride, an inhibitor of vacuolar proteases, resulted in significant reduction in clearance. Consistently, a cim3-1 yeast mutant restricted in the 19 S proteasome regulatory subunit was unaffected in clearance, whereas an Δatg1 yeast mutant deficient in autophagy showed a delayed aggregate clearance response. A cim3-1Δatg1 double mutant was still able to clear aggregates, suggesting additional cellular mechanisms for α-synuclein clearance. Our data provide insight into the mechanisms yeast cells use for clearing different species of α-synuclein and demonstrate a higher contribution of the autophagy/vacuole than the proteasome system. This contributes to the understanding of how cells can cope with toxic and/or aggregated proteins and may ultimately enable the development of novel strategies for therapeutic intervention."],["dc.identifier.doi","10.1074/jbc.M112.361865"],["dc.identifier.pmid","22722939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15838"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.title","Aggregate clearance of α-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1278"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","1295"],["dc.bibliographiccitation.volume","71"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Sari, Fatih"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, Stefan"],["dc.date.accessioned","2018-11-07T08:32:21Z"],["dc.date.available","2018-11-07T08:32:21Z"],["dc.date.issued","2009"],["dc.description.abstract","Spore formation is a common process in the developmental cycle of fungi. In the yeast Saccharomyces cerevisiae, Ime2 is a key protein kinase for the meiotic cell cycle, which precedes ascospore formation. Here, we analysed the IME2-related imeB gene of the filamentous ascomycete Aspergillus nidulans. imeB deletion strains are retarded in growth and overproduce fertile sexual fruiting bodies in the presence of light, which normally represses sexual development. imeB mutants also display abnormal differentiation of sexual Hulle cells in submerged cultures. Increased sexual development of imeB mutants is dependent on VeA, a component of the heterotrimeric velvet complex. A combined deletion of imeB with the phytochrome fphA, a red light receptor, results in a complete loss of light response, suggesting that ImeB and FphA cooperate in light-mediated inhibition of sexual development. Furthermore, we found that imeB mutants fail to produce the mycotoxin sterigmatocystin, an aflatoxin precursor, and show that ImeB is needed for expression of the sterigmatocystin gene cluster. ImeB contains a TXY motif conserved in mitogen-activated protein kinases. This sequence element is essential for ImeB function. We conclude that ImeB is a mitogen-activated protein kinase-related protein kinase required for the co-ordinated control of light-dependent development with mycotoxin production."],["dc.identifier.doi","10.1111/j.1365-2958.2009.06606.x"],["dc.identifier.isi","000263522000017"],["dc.identifier.pmid","19210625"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17324"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell Publishing, Inc"],["dc.relation.issn","0950-382X"],["dc.title","The protein kinase ImeB is required for light-mediated inhibition of sexual development and for mycotoxin production in Aspergillus nidulans"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","663"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","672"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Pries, R."],["dc.contributor.author","Bomeke, K."],["dc.contributor.author","Irniger, S."],["dc.contributor.author","Grundmann, O."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:58:04Z"],["dc.date.available","2018-11-07T09:58:04Z"],["dc.date.issued","2002"],["dc.description.abstract","The c-Jun-like transcriptional activator Gcn4p controls biosynthesis of translational precursors in the yeast Saccharomyces cerevisiae. Protein stability is dependent on amino acid limitation and cis signals within Gcn4p which are recognized by cyclin-dependent protein kinases, including Pho85p. The Gcn4p population within unstarved yeast consists of a small relatively stable cytoplasmic fraction and a larger less stable nuclear fraction. Gcn4p contains two nuclear localization signals (NLS) which function independently of the presence or absence of amino acids. Expression of NLS-truncated Gcn4p results in an increased cytoplasmic fraction and an overall stabilization of the protein. The same effect is achieved for the entire Gcn4p in a yrb1 yeast mutant strain impaired in the nuclear import machinery. In the presence of amino acids, controlled destabilization of Gcn4p is triggered by the phosphorylation activity of Pho85p. A pho85Delta mutation stabilizes Gcn4p without affecting nuclear import. Pho85p is localized within the nucleus in the presence or absence of amino acids. Therefore, there is a strict spatial separation of protein synthesis and degradation of Gcn4p in yeast. Control of protein stabilization which antagonizes Gcn4p function is restricted to the nucleus."],["dc.identifier.doi","10.1128/EC.1.5.663-672.2002"],["dc.identifier.isi","000178771200002"],["dc.identifier.pmid","12455686"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37293"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1535-9778"],["dc.title","Amino acid-dependent Gcn4p stability regulation occurs exclusively in the yeast nucleus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1002816"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Bayram, Özlem Sarikaya"],["dc.contributor.author","Ahmed, Yasar Luqman"],["dc.contributor.author","Maruyama, Jun-ichi"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Rizzoli, Silvio"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Irniger, Stefan"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2017-09-07T11:48:50Z"],["dc.date.available","2017-09-07T11:48:50Z"],["dc.date.issued","2012"],["dc.description.abstract","The sexual Fus3 MAP kinase module of yeast is highly conserved in eukaryotes and transmits external signals from the plasma membrane to the nucleus. We show here that the module of the filamentous fungus Aspergillus nidulans ( An) consists of the AnFus3 MAP kinase, the upstream kinases AnSte7 and AnSte11, and the AnSte50 adaptor. The fungal MAPK module controls the coordination of fungal development and secondary metabolite production. It lacks the membrane docking yeast Ste5 scaffold homolog; but, similar to yeast, the entire MAPK module's proteins interact with each other at the plasma membrane. AnFus3 is the only subunit with the potential to enter the nucleus from the nuclear envelope. AnFus3 interacts with the conserved nuclear transcription factor AnSte12 to initiate sexual development and phosphorylates VeA, which is a major regulatory protein required for sexual development and coordinated secondary metabolite production. Our data suggest that not only Fus3, but even the entire MAPK module complex of four physically interacting proteins, can migrate from plasma membrane to nuclear envelope."],["dc.identifier.doi","10.1371/journal.pgen.1002816"],["dc.identifier.gro","3142498"],["dc.identifier.isi","000306840400030"],["dc.identifier.pmid","22829779"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7871"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8856"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Aspergillus nidulans MAPK Module AnSte11-Ste50-Ste7-Fus3 Controls Development and Secondary Metabolism"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","38929"],["dc.bibliographiccitation.issue","49"],["dc.bibliographiccitation.journal","Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","38937"],["dc.bibliographiccitation.volume","275"],["dc.contributor.author","Baumer, M."],["dc.contributor.author","Kunzler, M."],["dc.contributor.author","Steigemann, P."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, S."],["dc.date.accessioned","2018-11-07T08:43:24Z"],["dc.date.available","2018-11-07T08:43:24Z"],["dc.date.issued","2000"],["dc.description.abstract","Ubiquitin dependent proteolysis of specific target proteins is required for several important steps during the cell cycle, Degradation of such proteins is strictly cell cycle-regulated and triggered by two large ubiquitin ligases, termed anaphase-promoting complex (APC) and Skp1/Cullin/F-box complex (SCF), Here we show that yeast Ran-binding protein 1 (Yrb1p), a predominantly cytoplasmic protein implicated in nucleocytoplasmic transport, is required for cell cycle regulated protein degradation. Depletion of Yrb1p results in the accumulation of unbudded G(1) cells and of cells arrested in mitosis implying a function of Yrb1p in the G(1)/S transition and in the progression through mitosis, Temperature-sensitive yrb1-51 mutants are defective in APC-mediated degradation of the anaphase inhibitor protein Pds1p and in degradation of the cyclin-dependent kinase inhibitor Sic1p, a target of SCF. Thus, Yrb1p is crucial for efficient APC- and SCF-mediated proteolysis of important cell cycle regulatory proteins. We have identified the UBS1 gene as a multicopy suppressor of yrb1-51 mutants. Ubs1p is a nuclear protein, and its deletion is synthetic lethal with a yrb1-51 mutation. Interestingly, UBS1 was previously identified as a multicopy suppressor of cdc34-2 mutants, which are defective in SCF activity. We suggest that Ubs1p may represent a link between nucleocytoplasmic transport and ubiquitin ligase activity."],["dc.identifier.doi","10.1074/jbc.M007925200"],["dc.identifier.isi","165739800107"],["dc.identifier.pmid","10991951"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19954"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1083-351X"],["dc.relation.issn","0021-9258"],["dc.title","Yeast Ran-binding protein Yrb1p is required for efficient proteolysis of cell cycle regulatory proteins Pds1p and Sic1p"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1001226"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Bayram, Oezlem Sarikaya"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Park, Hee Soo"],["dc.contributor.author","Irniger, Stefan"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Ni, Min"],["dc.contributor.author","Han, Kap-Hoon"],["dc.contributor.author","Yu, Jae-Hyuk"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T08:36:31Z"],["dc.date.available","2018-11-07T08:36:31Z"],["dc.date.issued","2010"],["dc.description.abstract","VeA is the founding member of the velvet superfamily of fungal regulatory proteins. This protein is involved in light response and coordinates sexual reproduction and secondary metabolism in Aspergillus nidulans. In the dark, VeA bridges VelB and LaeA to form the VelB-VeA-LaeA (velvet) complex. The VeA-like protein VelB is another developmental regulator, and LaeA has been known as global regulator of secondary metabolism. In this study, we show that VelB forms a second light-regulated developmental complex together with VosA, another member of the velvet family, which represses asexual development. LaeA plays a key role, not only in secondary metabolism, but also in directing formation of the VelB-VosA and VelB-VeA-LaeA complexes. LaeA controls VeA modification and protein levels and possesses additional developmental functions. The laeA null mutant results in constitutive sexual differentiation, indicating that LaeA plays a pivotal role in inhibiting sexual development in response to light. Moreover, the absence of LaeA results in the formation of significantly smaller fruiting bodies. This is due to the lack of a specific globose cell type (Hulle cells), which nurse the young fruiting body during development. This suggests that LaeA controls Hulle cells. In summary, LaeA plays a dynamic role in fungal morphological and chemical development, and it controls expression, interactions, and modification of the velvet regulators."],["dc.identifier.doi","10.1371/journal.pgen.1001226"],["dc.identifier.isi","000285578900004"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7265"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18331"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","LaeA Control of Velvet Family Regulatory Proteins for Light-Dependent Development and Fungal Cell-Type Specificity"],["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","142"],["dc.bibliographiccitation.issue","2-3"],["dc.bibliographiccitation.journal","FEBS Letters"],["dc.bibliographiccitation.lastpage","148"],["dc.bibliographiccitation.volume","468"],["dc.contributor.author","Baumer, M."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, S."],["dc.date.accessioned","2018-11-07T09:53:18Z"],["dc.date.available","2018-11-07T09:53:18Z"],["dc.date.issued","2000"],["dc.description.abstract","Sister chromatid separation and mitotic exit are triggered by the anaphase-promoting complex (APC/C) which is a multi-subunit ubiquitin ligase required for proteolytic degradation of various target proteins. Cdc20 and Cdh1 are substrate specific activators of the APC/C. It was previously proposed that Cdh1 is essential for proteolysis of the yeast mitotic cyclin Clb2. We show that Clb2 proteolysis is triggered by two different modes during mitosis. A fraction of Clb2 is degraded during anaphase in the absence of Cdh1. However a second fraction of Clb2 remains stable during anaphase and is degraded in a Cdh1-dependent manner as cells exit from mitosis, Most of cyclin Clb3 is degraded independently of Cdh1. Our data imply that degradation of mitotic cyclins is initiated by a Cdh1-independent mechanism. (C) 2000 Federation of European Biochemical Societies."],["dc.identifier.doi","10.1016/S0014-5793(00)01208-4"],["dc.identifier.isi","000085662000008"],["dc.identifier.pmid","10692575"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36302"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1873-3468"],["dc.relation.issn","0014-5793"],["dc.title","Two different modes of cyclin Clb2 proteolysis during mitosis in Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2611"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Cell Cycle"],["dc.bibliographiccitation.lastpage","2619"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Kuczera, Tanja"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Sari, Fatih"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Irniger, Stefan"],["dc.date.accessioned","2018-11-07T08:41:34Z"],["dc.date.available","2018-11-07T08:41:34Z"],["dc.date.issued","2010"],["dc.description.abstract","Progression through mitosis requires the activity of cyclin-dependent kinases (CDKs) associated with regulatory cyclin subunits. In the yeast Saccharomyces cerevisiae, Clb2 has the most important role among the four mitotic cyclins, Clb1-4, manifested by data showing that simultaneous deletion of the CLB1, CLB3 and CLB4 genes has only minor effects on mitosis. Thus, Clb2 alone is sufficient for all essential CDK functions in mitosis, such as the assembly of bipolar spindles and spindle elongation. Here, we show that a modification of Clb2, by the C-terminal addition of a Myc12 epitope, causes the loss of one specific mitotic function of Clb2. Strains carrying CLB2-MYC12 are nonviable in the absence of the CLB3 and CLB4 genes, because the modified Clb2 version fails to promote assembly of the mitotic spindle. In contrast, Clb2-Myc12 has no apparent defects in late mitotic functions and, furthermore, induces the switch from polarized to isotropic growth with similar efficiency as the endogenous Clb2. Thus, the presence of the Myc12 epitope selectively inactivates Clb2's capacity to promote spindle formation. Clb2-Myc12 represents therefore the first version of Clb2 impaired in one specific mitotic function. We conclude that the major mitotic functions of this cyclin can be unequivocally dissected."],["dc.identifier.doi","10.4161/cc.9.13.12082"],["dc.identifier.isi","000281205400035"],["dc.identifier.pmid","20581451"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19497"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Inc"],["dc.relation.issn","1551-4005"],["dc.relation.issn","1538-4101"],["dc.title","Dissection of mitotic functions of the yeast cyclin Clb2"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]