Braus, Gerhard H.

[["dc.bibliographiccitation.journal","Frontiers in Fungal Biology"],["dc.bibliographiccitation.volume","2"],["dc.contributor.affiliation","Gerke, Jennifer; 1Department of Moleuclar Microbiology and Genetics and Göttingen Center for Molecular Biosciences (GZMB), Georg-August-Universität Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Köhler, Anna M.; 1Department of Moleuclar Microbiology and Genetics and Göttingen Center for Molecular Biosciences (GZMB), Georg-August-Universität Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Wennrich, Jan-Peer; 2Microbial Drugs Department, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany"],["dc.contributor.affiliation","Große, Verena; 1Department of Moleuclar Microbiology and Genetics and Göttingen Center for Molecular Biosciences (GZMB), Georg-August-Universität Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Shao, Lulu; 2Microbial Drugs Department, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany"],["dc.contributor.affiliation","Heinrich, Antje K.; 4Molecular Biotechnology, Goethe University Frankfurt, Frankfurt am Main, Germany"],["dc.contributor.affiliation","Bode, Helge B.; 4Molecular Biotechnology, Goethe University Frankfurt, Frankfurt am Main, Germany"],["dc.contributor.affiliation","Chen, Wanping; 1Department of Moleuclar Microbiology and Genetics and Göttingen Center for Molecular Biosciences (GZMB), Georg-August-Universität Göttingen, Göttingen, Germany"],["dc.contributor.affiliation","Surup, Frank; 2Microbial Drugs Department, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany"],["dc.contributor.affiliation","Braus, Gerhard H.; 1Department of Moleuclar Microbiology and Genetics and Göttingen Center for Molecular Biosciences (GZMB), Georg-August-Universität Göttingen, Göttingen, Germany"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Köhler, Anna M."],["dc.contributor.author","Wennrich, Jan-Peer"],["dc.contributor.author","Große, Verena"],["dc.contributor.author","Shao, Lulu"],["dc.contributor.author","Heinrich, Antje K."],["dc.contributor.author","Bode, Helge B."],["dc.contributor.author","Chen, Wanping"],["dc.contributor.author","Surup, Frank"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2022-09-05T09:05:07Z"],["dc.date.available","2022-09-05T09:05:07Z"],["dc.date.issued","2022-01-03"],["dc.date.updated","2022-09-04T05:12:06Z"],["dc.description.abstract","The soil microbiome comprises numerous filamentous fungi and bacteria that mutually react and challenge each other by the production of bioactive secondary metabolites. Herein, we show in liquid co-cultures that the presence of filamentous Streptomycetes producing antifungal glycopeptide antibiotics induces the production of the antibacterial and iron-chelating tropolones anhydrosepedonin (1) and antibiotic C (2) in the mold Aspergillus nidulans. Additionally, the biosynthesis of the related polyketide tripyrnidone (5) was induced, whose novel tricyclic scaffold we elucidated by NMR and HRESIMS data. The corresponding biosynthetic polyketide synthase-encoding gene cluster responsible for the production of these compounds was identified. The tropolones as well as tripyrnidone (5) are produced by genes that belong to the broad reservoir of the fungal genome for the synthesis of different secondary metabolites, which are usually silenced under standard laboratory conditions. These molecules might be part of the bacterium-fungus competition in the complex soil environment, with the bacterial glycopeptide antibiotic as specific environmental trigger for fungal induction of this cluster."],["dc.identifier.doi","10.3389/ffunb.2021.777474"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/114077"],["dc.language.iso","en"],["dc.relation.eissn","2673-6128"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0/"],["dc.title","Biosynthesis of Antibacterial Iron-Chelating Tropolones in Aspergillus nidulans as Response to Glycopeptide-Producing Streptomycetes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","mBio"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Troppens, Danielle M."],["dc.contributor.author","Köhler, Anna M."],["dc.contributor.author","Schlüter, Rabea"],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.editor","Di Pietro, Antonio"],["dc.date.accessioned","2021-04-14T08:24:02Z"],["dc.date.available","2021-04-14T08:24:02Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1128/mBio.01673-20"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81142"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","2150-7511"],["dc.title","Hülle Cells of Aspergillus nidulans with Nuclear Storage and Developmental Backup Functions Are Reminiscent of Multipotent Stem Cells"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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.artnumber","238"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Biomolecules"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Meister, Cindy"],["dc.contributor.author","Thieme, Karl G."],["dc.contributor.author","Thieme, Sabine"],["dc.contributor.author","Köhler, Anna M."],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2019-09-24T07:24:10Z"],["dc.date.available","2019-09-24T07:24:10Z"],["dc.date.issued","2019"],["dc.description.abstract","COP9 signalosome (CSN) and Den1/A deneddylases physically interact and promote multicellular development in fungi. CSN recognizes Skp1/cullin-1/Fbx E3 cullin-RING ligases (CRLs) without substrate and removes their posttranslational Nedd8 modification from the cullin scaffold. This results in CRL complex disassembly and allows Skp1 adaptor/Fbx receptor exchange for altered substrate specificity. We characterized the novel ubiquitin-specific protease UspA of the mold Aspergillusnidulans, which corresponds to CSN-associated human Usp15 and interacts with six CSN subunits. UspA reduces amounts of ubiquitinated proteins during fungal development, and the uspA gene expression is repressed by an intact CSN. UspA is localized in proximity to nuclei and recruits proteins related to nuclear transport and transcriptional processing, suggesting functions in nuclear entry control. UspA accelerates the formation of asexual conidiospores, sexual development, and supports the repression of secondary metabolite clusters as the derivative of benzaldehyde (dba) genes. UspA reduces protein levels of the fungal NF-kappa B-like velvet domain protein VeA, which coordinates differentiation and secondary metabolism. VeA stability depends on the Fbx23 receptor, which is required for light controlled development. Our data suggest that the interplay between CSN deneddylase, UspA deubiquitinase, and SCF-Fbx23 ensures accurate levels of VeA to support fungal development and an appropriate secondary metabolism."],["dc.identifier.doi","10.3390/biom9060238"],["dc.identifier.pmid","31216760"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16253"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62435"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation.eissn","2218-273X"],["dc.relation.issn","2218-273X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","COP9 Signalosome Interaction with UspA/Usp15 Deubiquitinase Controls VeA-Mediated Fungal Multicellular Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]