Valerius, Oliver

[["dc.bibliographiccitation.artnumber","e1007511"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Thieme, Karl G."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Sasse, Christoph"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Thieme, Sabine"],["dc.contributor.author","Karimi, Razieh"],["dc.contributor.author","Heinrich, Antje K."],["dc.contributor.author","Finkernagel, Florian"],["dc.contributor.author","Smith, Kristina"],["dc.contributor.author","Bode, Helge B."],["dc.contributor.author","Freitag, Michael"],["dc.contributor.author","Ram, Arthur F. J."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2019-07-09T11:45:46Z"],["dc.date.available","2019-07-09T11:45:46Z"],["dc.date.issued","2018"],["dc.description.abstract","The NF-κB-like velvet domain protein VosA (viability of spores) binds to more than 1,500 promoter sequences in the filamentous fungus Aspergillus nidulans. VosA inhibits premature induction of the developmental activator gene brlA, which promotes asexual spore formation in response to environmental cues as light. VosA represses a novel genetic network controlled by the sclB gene. SclB function is antagonistic to VosA, because it induces the expression of early activator genes of asexual differentiation as flbC and flbD as well as brlA. The SclB controlled network promotes asexual development and spore viability, but is independent of the fungal light control. SclB interactions with the RcoA transcriptional repressor subunit suggest additional inhibitory functions on transcription. SclB links asexual spore formation to the synthesis of secondary metabolites including emericellamides, austinol as well as dehydroaustinol and activates the oxidative stress response of the fungus. The fungal VosA-SclB regulatory system of transcription includes a VosA control of the sclB promoter, common and opposite VosA and SclB control functions of fungal development and several additional regulatory genes. The relationship between VosA and SclB illustrates the presence of a convoluted surveillance apparatus of transcriptional control, which is required for accurate fungal development and the linkage to the appropriate secondary metabolism."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2018"],["dc.identifier.doi","10.1371/journal.pgen.1007511"],["dc.identifier.pmid","30044771"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15315"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59309"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.subject.ddc","570"],["dc.title","Velvet domain protein VosA represses the zinc cluster transcription factor SclB regulatory network for Aspergillus nidulans asexual development, oxidative stress response and secondary metabolism."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1009434"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Höfer, Annalena M."],["dc.contributor.author","Harting, Rebekka"],["dc.contributor.author","Aßmann, Nils F."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Starke, Jessica"],["dc.contributor.author","Bayram, Özgür"],["dc.contributor.author","Tran, Van-Tuan"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-04-14T08:28:05Z"],["dc.date.available","2021-04-14T08:28:05Z"],["dc.date.issued","2021"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1371/journal.pgen.1009434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82499"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.rights","CC BY 4.0"],["dc.title","The velvet protein Vel1 controls initial plant root colonization and conidia formation for xylem distribution in Verticillium wilt"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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.issue","3"],["dc.bibliographiccitation.journal","mBio"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Köhler, Anna M."],["dc.contributor.author","Harting, Rebekka"],["dc.contributor.author","Langeneckert, Annika E."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Meister, Cindy"],["dc.contributor.author","Strohdiek, Anja"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.editor","Di Pietro, Antonio"],["dc.date.accessioned","2020-12-10T18:37:04Z"],["dc.date.available","2020-12-10T18:37:04Z"],["dc.date.issued","2019"],["dc.description.abstract","E3 cullin-RING ubiquitin ligase (CRL) complexes recognize specific substrates and are activated by covalent modification with ubiquitin-like Nedd8. Deneddylation inactivates CRLs and allows Cand1/A to bind and exchange substrate recognition subunits. Human as well as most fungi possess a single gene for the receptor exchange factor Cand1, which is split and rearranged in aspergilli into two genes for separate proteins. Aspergillus nidulans CandA-N blocks the neddylation site, and CandA-C inhibits the interaction to the adaptor/substrate receptor subunits similar to the respective N-terminal and C-terminal parts of single Cand1. The pathogen Aspergillus fumigatus and related species express a CandA-C with a 190-amino-acid N-terminal extension domain encoded by an additional exon. This extension corresponds in most aspergilli, including A. nidulans, to a gene directly upstream of candA-C encoding a 20-kDa protein without human counterpart. This protein was named CandA-C1, because it is also required for the cellular deneddylation/neddylation cycle and can form a trimeric nuclear complex with CandA-C and CandA-N. CandA-C and CandA-N are required for asexual and sexual development and control a distinct secondary metabolism. CandA-C1 and the corresponding domain of A. fumigatus control spore germination, vegetative growth, and the repression of additional secondary metabolites. This suggests that the dissection of the conserved Cand1-encoding gene within the genome of aspergilli was possible because it allowed the integration of a fungus-specific protein required for growth into the CandA complex in two different gene set versions, which might provide an advantage in evolution.IMPORTANCEAspergillus species are important for biotechnological applications, like the production of citric acid or antibacterial agents. Aspergilli can cause food contamination or invasive aspergillosis to immunocompromised humans or animals. Specific treatment is difficult due to limited drug targets and emerging resistances. The CandA complex regulates, as a receptor exchange factor, the activity and substrate variability of the ubiquitin labeling machinery for 26S proteasome-mediated protein degradation. Only Aspergillus species encode at least two proteins that form a CandA complex. This study shows that Aspergillus species had to integrate a third component into the CandA receptor exchange factor complex that is unique to aspergilli and required for vegetative growth, sexual reproduction, and activation of the ubiquitin labeling machinery. These features have interesting implications for the evolution of protein complexes and could make CandA-C1 an interesting candidate for target-specific drug design to control fungal growth without affecting the human ubiquitin-proteasome system."],["dc.identifier.doi","10.1128/mBio.01094-19"],["dc.identifier.eissn","2150-7511"],["dc.identifier.pmid","31213557"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16203"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76828"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2150-7511"],["dc.relation.issn","2150-7511"],["dc.rights","CC BY 4.0"],["dc.title","Integration of Fungus-Specific CandA-C1 into a Trimeric CandA Complex Allowed Splitting of the Gene for the Conserved Receptor Exchange Factor of CullinA E3 Ubiquitin Ligases in Aspergilli"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Liu, Li"],["dc.contributor.author","Sasse, Christoph"],["dc.contributor.author","Dirnberger, Benedict"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Fekete-Szücs, Enikő"],["dc.contributor.author","Harting, Rebekka"],["dc.contributor.author","Nordzieke, Daniela E"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.contributor.author","Karlovsky, Petr"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Braus, Gerhard H"],["dc.date.accessioned","2021-12-01T09:24:08Z"],["dc.date.available","2021-12-01T09:24:08Z"],["dc.date.issued","2021"],["dc.description.abstract","Fungal Hülle cells with nuclear storage and developmental backup functions are reminiscent of multipotent stem cells. In the soil, Hülle cells nurse the overwintering fruiting bodies of Aspergillus nidulans . The genome of A. nidulans harbors genes for the biosynthesis of xanthones. We show that enzymes and metabolites of this biosynthetic pathway accumulate in Hülle cells under the control of the regulatory velvet complex, which coordinates development and secondary metabolism. Deletion strains blocked in the conversion of anthraquinones to xanthones accumulate emodins and are delayed in maturation and growth of fruiting bodies. Emodin represses fruiting body and resting structure formation in other fungi. Xanthones are not required for sexual development but exert antifeedant effects on fungivorous animals such as springtails and woodlice. Our findings reveal a novel role of Hülle cells in establishing secure niches for A. nidulans by accumulating metabolites with antifeedant activity that protect reproductive structures from animal predators."],["dc.description.abstract","Fungal Hülle cells with nuclear storage and developmental backup functions are reminiscent of multipotent stem cells. In the soil, Hülle cells nurse the overwintering fruiting bodies of Aspergillus nidulans . The genome of A. nidulans harbors genes for the biosynthesis of xanthones. We show that enzymes and metabolites of this biosynthetic pathway accumulate in Hülle cells under the control of the regulatory velvet complex, which coordinates development and secondary metabolism. Deletion strains blocked in the conversion of anthraquinones to xanthones accumulate emodins and are delayed in maturation and growth of fruiting bodies. Emodin represses fruiting body and resting structure formation in other fungi. Xanthones are not required for sexual development but exert antifeedant effects on fungivorous animals such as springtails and woodlice. Our findings reveal a novel role of Hülle cells in establishing secure niches for A. nidulans by accumulating metabolites with antifeedant activity that protect reproductive structures from animal predators."],["dc.identifier.doi","10.7554/eLife.68058"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94858"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2050-084X"],["dc.title","Secondary metabolites of Hülle cells mediate protection of fungal reproductive and overwintering structures against fungivorous animals"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","964"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","979"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Nahlik, Krystyna"],["dc.contributor.author","Dumkow, Marc"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Helmstaedt, Kerstin"],["dc.contributor.author","Busch, Silke"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Schwier, Elke U."],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Westermann, Mieke"],["dc.contributor.author","Grond, Stephanie"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T09:12:22Z"],["dc.date.available","2018-09-28T09:12:22Z"],["dc.date.issued","2010"],["dc.description.abstract","The COP9 signalosome complex (CSN) is a crucial regulator of ubiquitin ligases. Defects in CSN result in embryonic impairment and death in higher eukaryotes, whereas the filamentous fungus Aspergillus nidulans survives without CSN, but is unable to complete sexual development. We investigated overall impact of CSN activity on A. nidulans cells by combined transcriptome, proteome and metabolome analysis. Absence of csn5/csnE affects transcription of at least 15% of genes during development, including numerous oxidoreductases. csnE deletion leads to changes in the fungal proteome indicating impaired redox regulation and hypersensitivity to oxidative stress. CSN promotes the formation of asexual spores by regulating developmental hormones produced by PpoA and PpoC dioxygenases. We identify more than 100 metabolites, including orsellinic acid derivatives, accumulating preferentially in the csnE mutant. We also show that CSN is required to activate glucanases and other cell wall recycling enzymes during development. These findings suggest a dual role for CSN during development: it is required early for protection against oxidative stress and hormone regulation and is later essential for control of the secondary metabolism and cell wall rearrangement."],["dc.identifier.doi","10.1111/j.1365-2958.2010.07384.x"],["dc.identifier.pmid","21062371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15841"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1365-2958"],["dc.title","The COP9 signalosome mediates transcriptional and metabolic response to hormones, oxidative stress protection and cell wall rearrangement during fungal development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1005205"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","PLoS Pathogens"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Lin, Chi-Jan"],["dc.contributor.author","Sasse, Christoph"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Irmer, Henriette"],["dc.contributor.author","Frauendorf, Holm"],["dc.contributor.author","Heinekamp, Thorsten"],["dc.contributor.author","Strassburger, Maria"],["dc.contributor.author","van Tuan Tran, Van Tuan Tran"],["dc.contributor.author","Herzog, Britta"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:49:12Z"],["dc.date.available","2018-11-07T09:49:12Z"],["dc.date.issued","2015"],["dc.description.abstract","The transcription factor Flo8/Som1 controls filamentous growth in Saccharomyces cerevisiae and virulence in the plant pathogen Magnaporthe oryzae. Flo8/Som1 includes a characteristic N-terminal LUG/LUH-Flo8-single-stranded DNA binding (LUFS) domain and is activated by the cAMP dependent protein kinase A signaling pathway. Heterologous SomA from Aspergillus fumigatus rescued in yeast flo8 mutant strains several phenotypes including adhesion or flocculation in haploids and pseudohyphal growth in diploids, respectively. A. fumigatus SomA acts similarly to yeast Flo8 on the promoter of FLO11 fused with reporter gene (LacZ) in S. cerevisiae. FLO11 expression in yeast requires an activator complex including Flo8 and Mfg1. Furthermore, SomA physically interacts with PtaB, which is related to yeast Mfg1. Loss of the somA gene in A. fumigatus resulted in a slow growth phenotype and a block in asexual development. Only aerial hyphae without further differentiation could be formed. The deletion phenotype was verified by a conditional expression of somA using the inducible Tet-on system. A adherence assay with the conditional somA expression strain indicated that SomA is required for biofilm formation. A ptaB deletion strain showed a similar phenotype supporting that the SomA/PtaB complex controls A. fumigatus biofilm formation. Transcriptional analysis showed that SomA regulates expression of genes for several transcription factors which control conidiation or adhesion of A. fumigatus. Infection assays with fertilized chicken eggs as well as with mice revealed that SomA is required for pathogenicity. These data corroborate a complex control function of SomA acting as a central factor of the transcriptional network, which connects adhesion, spore formation and virulence in the opportunistic human pathogen A. fumigatus."],["dc.description.sponsorship","Open-Access Publikationsfonds 2015"],["dc.identifier.doi","10.1371/journal.ppat.1005205"],["dc.identifier.isi","000368332000007"],["dc.identifier.pmid","26529322"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12564"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/35459"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7374"],["dc.relation.issn","1553-7366"],["dc.rights.access","openAccess"],["dc.title","Transcription Factor SomA Is Required for Adhesion, Development and Virulence of the Human Pathogen Aspergillus fumigatus"],["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"]]