Braus, Gerhard H.

[["dc.bibliographiccitation.journal","Frontiers in Microbiology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Horta, Maria Augusta C."],["dc.contributor.author","Thieme, Nils"],["dc.contributor.author","Gao, Yuqian"],["dc.contributor.author","Burnum-Johnson, Kristin E."],["dc.contributor.author","Nicora, Carrie D."],["dc.contributor.author","Gritsenko, Marina A."],["dc.contributor.author","Lipton, Mary S."],["dc.contributor.author","Mohanraj, Karthikeyan"],["dc.contributor.author","de Assis, Leandro José"],["dc.contributor.author","Lin, Liangcai"],["dc.contributor.author","Tian, Chaoguang"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Borkovich, Katherine A."],["dc.contributor.author","Schmoll, Monika"],["dc.contributor.author","Larrondo, Luis F."],["dc.contributor.author","Samal, Areejit"],["dc.contributor.author","Goldman, Gustavo H."],["dc.contributor.author","Benz, J. Philipp"],["dc.date.accessioned","2020-12-10T18:44:28Z"],["dc.date.available","2020-12-10T18:44:28Z"],["dc.date.issued","2019"],["dc.description.abstract","Fungal plant cell wall degradation processes are governed by complex regulatory mechanisms, allowing the organisms to adapt their metabolic program with high specificity to the available substrates. While the uptake of representative plant cell wall mono- and disaccharides is known to induce specific transcriptional and translational responses, the processes related to early signal reception and transduction remain largely unknown. A fast and reversible way of signal transmission are post-translational protein modifications, such as phosphorylations, which could initiate rapid adaptations of the fungal metabolism to a new condition. To elucidate how changes in the initial substrate recognition phase of Neurospora crassa affect the global phosphorylation pattern, phospho-proteomics was performed after a short (2 min) induction period with several plant cell wall-related mono- and disaccharides. The MS/MS-based peptide analysis revealed large-scale substrate-specific protein phosphorylation and de-phosphorylations. Using the proteins identified by MS/MS, a protein-protein-interaction (PPI) network was constructed. The variance in phosphorylation of a large number of kinases, phosphatases and transcription factors indicate the participation of many known signaling pathways, including circadian responses, two-component regulatory systems, MAP kinases as well as the cAMP-dependent and heterotrimeric G-protein pathways. Adenylate cyclase, a key component of the cAMP pathway, was identified as a potential hub for carbon source-specific differential protein interactions. In addition, four phosphorylated F-Box proteins were identified, two of which, Fbx-19 and Fbx-22, were found to be involved in carbon catabolite repression responses. Overall, these results provide unprecedented and detailed insights into a so far less well known stage of the fungal response to environmental cues and allow to better elucidate the molecular mechanisms of sensory perception and signal transduction during plant cell wall degradation."],["dc.identifier.doi","10.3389/fmicb.2019.02317"],["dc.identifier.eissn","1664-302X"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78463"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","Frontiers Media S.A."],["dc.relation.eissn","1664-302X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Broad Substrate-Specific Phosphorylation Events Are Associated With the Initial Stage of Plant Cell Wall Recognition in Neurospora crassa"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1007141"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Heinrich, Gabriele"],["dc.contributor.author","Gross, Carina"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Braus, Gerhard H."],["dc.creator.editor","Brakhage, Axel A."],["dc.date.accessioned","2018-04-23T11:47:09Z"],["dc.date.available","2018-04-23T11:47:09Z"],["dc.date.issued","2018"],["dc.description.abstract","The transition from vegetative growth to multicellular development represents an evolutionary hallmark linked to an oxidative stress signal and controlled protein degradation. We identified the Sem1 proteasome subunit, which connects stress response and cellular differentiation. The sem1 gene encodes the fungal counterpart of the human Sem1 proteasome lid subunit and is essential for fungal cell differentiation and development. A sem1 deletion strain of the filamentous fungus Aspergillus nidulans is able to grow vegetatively and expresses an elevated degree of 20S proteasomes with multiplied ATP-independent catalytic activity compared to wildtype. Oxidative stress induces increased transcription of the genes sem1 and rpn11 for the proteasomal deubiquitinating enzyme. Sem1 is required for stabilization of the Rpn11 deubiquitinating enzyme, incorporation of the ubiquitin receptor Rpn10 into the 19S regulatory particle and efficient 26S proteasome assembly. Sem1 maintains high cellular NADH levels, controls mitochondria integrity during stress and developmental transition."],["dc.identifier.doi","10.1371/journal.pgen.1007141"],["dc.identifier.gro","3142187"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15668"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13306"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Sem1 links proteasome stability and specificity to multicellular development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","6"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Fungal Biology and Biotechnology"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Meyer, Vera"],["dc.contributor.author","Andersen, Mikael R."],["dc.contributor.author","Brakhage, Axel A."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Caddick, Mark X."],["dc.contributor.author","Cairns, Timothy C."],["dc.contributor.author","de Vries, Ronald P."],["dc.contributor.author","Haarmann, Thomas"],["dc.contributor.author","Hansen, Kim"],["dc.contributor.author","Hertz-Fowler, Christiane"],["dc.contributor.author","Krappmann, Sven"],["dc.contributor.author","Mortensen, Uffe H."],["dc.contributor.author","Peñalva, Miguel A."],["dc.contributor.author","Ram, Arthur F. J."],["dc.contributor.author","Head, Ritchie M."],["dc.date.accessioned","2019-07-09T11:42:51Z"],["dc.date.available","2019-07-09T11:42:51Z"],["dc.date.issued","2016"],["dc.description.abstract","Abstract The EUROFUNG network is a virtual centre of multidisciplinary expertise in the field of fungal biotechnology. The first academic-industry Think Tank was hosted by EUROFUNG to summarise the state of the art and future challenges in fungal biology and biotechnology in the coming decade. Currently, fungal cell factories are important for bulk manufacturing of organic acids, proteins, enzymes, secondary metabolites and active pharmaceutical ingredients in white and red biotechnology. In contrast, fungal pathogens of humans kill more people than malaria or tuberculosis. Fungi are significantly impacting on global food security, damaging global crop production, causing disease in domesticated animals, and spoiling an estimated 10 % of harvested crops. A number of challenges now need to be addressed to improve our strategies to control fungal pathogenicity and to optimise the use of fungi as sources for novel compounds and as cell factories for large scale manufacture of bio-based products. This white paper reports on the discussions of the Think Tank meeting and the suggestions made for moving fungal bio(techno)logy forward."],["dc.identifier.doi","10.1186/s40694-016-0024-8"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13875"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58764"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Current challenges of research on filamentous fungi in relation to human welfare and a sustainable bio-economy: a white paper"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Frontiers in Molecular Neuroscience"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Rajavel, Abirami"],["dc.contributor.author","Dhamotharan, Karthikeyan"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Uhrig, Joachim F."],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2021-06-01T09:42:26Z"],["dc.date.available","2021-06-01T09:42:26Z"],["dc.date.issued","2021"],["dc.description.abstract","Aggregation of α-synuclein (αSyn) into proteinaceous deposits is a pathological hallmark of a range of neurodegenerative diseases including Parkinson’s disease (PD). Numerous lines of evidence indicate that the accumulation of toxic oligomeric and prefibrillar αSyn species may underpin the cellular toxicity and spread of pathology between cells. Therefore, aggregation of αSyn is considered a priority target for drug development, as aggregation inhibitors are expected to reduce αSyn toxicity and serve as therapeutic agents. Here, we used the budding yeast S. cerevisiae as a platform for the identification of short peptides that inhibit αSyn aggregation and toxicity. A library consisting of approximately one million peptide variants was utilized in two high-throughput screening approaches for isolation of library representatives that reduce αSyn-associated toxicity and aggregation. Seven peptides were isolated that were able to suppress specifically αSyn toxicity and aggregation in living cells. Expression of the peptides in yeast reduced the accumulation of αSyn-induced reactive oxygen species and increased cell viability. Next, the peptides were chemically synthesized and probed for their ability to modulate αSyn aggregation in vitro . Two synthetic peptides, K84s and K102s, of 25 and 19 amino acids, respectively, significantly inhibited αSyn oligomerization and aggregation at sub-stoichiometric molar ratios. Importantly, K84s reduced αSyn aggregation in human cells. These peptides represent promising αSyn aggregation antagonists for the development of future therapeutic interventions."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3389/fnmol.2021.659926"],["dc.identifier.pmid","33912013"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17845"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85254"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/420"],["dc.notes.intern","DOI-Import GROB-425"],["dc.notes.intern","Merged from goescholar"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["dc.relation.eissn","1662-5099"],["dc.relation.workinggroup","RG Outeiro (Experimental Neurodegeneration)"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation"],["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","e1001750"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Ahmed, Yasar Luqman"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Park, Hee-Soo"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Ni, Min"],["dc.contributor.author","Dickmanns, Achim"],["dc.contributor.author","Kim, Sun Chang"],["dc.contributor.author","Yu, Jae-Hyuk"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Ficner, Ralf"],["dc.date.accessioned","2017-09-07T11:47:00Z"],["dc.date.available","2017-09-07T11:47:00Z"],["dc.date.issued","2013"],["dc.description.abstract","Morphological development of fungi and their combined production of secondary metabolites are both acting in defence and protection. These processes are mainly coordinated by velvet regulators, which contain a yet functionally and structurally uncharacterized velvet domain. Here we demonstrate that the velvet domain of VosA is a novel DNA-binding motif that specifically recognizes an 11-nucleotide consensus sequence consisting of two motifs in the promoters of key developmental regulatory genes. The crystal structure analysis of the VosA velvet domain revealed an unforeseen structural similarity with the Rel homology domain (RHD) of the mammalian transcription factor NF-B. Based on this structural similarity several conserved amino acid residues present in all velvet domains have been identified and shown to be essential for the DNA binding ability of VosA. The velvet domain is also involved in dimer formation as seen in the solved crystal structures of the VosA homodimer and the VosA-VelB heterodimer. These findings suggest that defence mechanisms of both fungi and animals might be governed by structurally related DNA-binding transcription factors."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2013"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pbio.1001750"],["dc.identifier.gro","3142241"],["dc.identifier.isi","000329367200028"],["dc.identifier.pmid","24391470"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9579"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6098"],["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","1545-7885"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Velvet Family of Fungal Regulators Contains a DNA-Binding Domain Structurally Similar to NF-κB"],["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.artnumber","e1005899"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLoS Pathogens"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Joehnk, Bastian"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Abelmann, Anja"],["dc.contributor.author","Heinekamp, Thorsten"],["dc.contributor.author","Mattern, Derek J."],["dc.contributor.author","Brakhage, Axel A."],["dc.contributor.author","Jacobsen, Ilse D."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T10:09:12Z"],["dc.date.available","2018-11-07T10:09:12Z"],["dc.date.issued","2016"],["dc.description.abstract","F-box proteins share the F-box domain to connect substrates of E3 SCF ubiquitin RING ligases through the adaptor Skp1/A to Cul1/A scaffolds. F-box protein Fbx15 is part of the general stress response of the human pathogenic mold Aspergillus fumigatus. Oxidative stress induces a transient peak of fbx15 expression, resulting in 3x elevated Fbx15 protein levels. During non-stress conditions Fbx15 is phosphorylated and F-box mediated interaction with SkpA preferentially happens in smaller subpopulations in the cytoplasm. The F-box of Fbx15 is required for an appropriate oxidative stress response, which results in rapid dephosphorylation of Fbx15 and a shift of the cellular interaction with SkpA to the nucleus. Fbx15 binds SsnF/Ssn6 as part of the RcoA/Tup1-SsnF/Ssn6 co-repressor and is required for its correct nuclear localization. Dephosphorylated Fbx15 prevents SsnF/Ssn6 nuclear localization and results in the derepression of gliotoxin gene expression. fbx15 deletion mutants are unable to infect immunocompromised mice in a model for invasive aspergillosis. Fbx15 has a novel dual molecular function by controlling transcriptional repression and being part of SCF E3 ubiquitin ligases, which is essential for stress response, gliotoxin production and virulence in the opportunistic human pathogen A. fumigatus."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (DFG) [FOR1334, SFB860, BR1502/11-2]"],["dc.identifier.doi","10.1371/journal.ppat.1005899"],["dc.identifier.isi","000385621900056"],["dc.identifier.pmid","27649508"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13763"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/39611"],["dc.notes.intern","Merged from goescholar"],["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","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","SCF Ubiquitin Ligase F-box Protein Fbx15 Controls Nuclear Co-repressor Localization, Stress Response 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"]]

[["dc.bibliographiccitation.journal","Molecular Plant Pathology"],["dc.contributor.author","Harting, Rebekka"],["dc.contributor.author","Starke, Jessica"],["dc.contributor.author","Kusch, Harald"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.contributor.author","Maurus, Isabel"],["dc.contributor.author","Schlüter, Rabea"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Bulla, Ingo"],["dc.contributor.author","Nowrousian, Minou"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","de Jonge, Ronnie"],["dc.contributor.author","Stahlhut, Gertrud"],["dc.contributor.author","Hoff, Katharina J."],["dc.contributor.author","Aßhauer, Kathrin P."],["dc.contributor.author","Thürmer, Andrea"],["dc.contributor.author","Stanke, Mario"],["dc.contributor.author","Daniel, Rolf"],["dc.contributor.author","Morgenstern, Burkhard"],["dc.contributor.author","Thomma, Bart P. H. J."],["dc.contributor.author","Kronstad, James W."],["dc.contributor.author","Braus‐Stromeyer, Susanna A."],["dc.date.accessioned","2021-06-01T09:42:04Z"],["dc.date.available","2021-06-01T09:42:04Z"],["dc.date.issued","2021"],["dc.description.abstract","Abstract Amphidiploid fungal Verticillium longisporum strains Vl43 and Vl32 colonize the plant host Brassica napus but differ in their ability to cause disease symptoms. These strains represent two V. longisporum lineages derived from different hybridization events of haploid parental Verticillium strains. Vl32 and Vl43 carry same‐sex mating‐type genes derived from both parental lineages. Vl32 and Vl43 similarly colonize and penetrate plant roots, but asymptomatic Vl32 proliferation in planta is lower than virulent Vl43. The highly conserved Vl43 and Vl32 genomes include less than 1% unique genes, and the karyotypes of 15 or 16 chromosomes display changed genetic synteny due to substantial genomic reshuffling. A 20 kb Vl43 lineage‐specific (LS) region apparently originating from the Verticillium dahliae‐related ancestor is specific for symptomatic Vl43 and encodes seven genes, including two putative transcription factors. Either partial or complete deletion of this LS region in Vl43 did not reduce virulence but led to induction of even more severe disease symptoms in rapeseed. This suggests that the LS insertion in the genome of symptomatic V. longisporum Vl43 mediates virulence‐reducing functions, limits damage on the host plant, and therefore tames Vl43 from being even more virulent."],["dc.description.abstract","A lineage‐specific region in the Verticillium longisporum Vl43 genome reduces fungal virulence of infected rapeseed host plants. image"],["dc.description.sponsorship","Bundesministerium für Bildung und Forschung: BioFung http://dx.doi.org/10.13039/501100002347"],["dc.description.sponsorship","Natural Sciences and Engineering Research Council of Canada: CREATE http://dx.doi.org/10.13039/501100000038"],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.1111/mpp.13071"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/85132"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-425"],["dc.relation.eissn","1364-3703"],["dc.relation.issn","1464-6722"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","A 20‐kb lineage‐specific genomic region tames virulence in pathogenic amphidiploid Verticillium longisporum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","e1006098"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLOS Genetics"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Kleinknecht, Alexandra"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Pinho, Raquel"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.editor","Lu, Bingwei"],["dc.date.accessioned","2018-09-28T07:41:43Z"],["dc.date.available","2018-09-28T07:41:43Z"],["dc.date.issued","2016"],["dc.description.abstract","Parkinson´s disease (PD) is characterized by the presence of proteinaceous inclusions called Lewy bodies that are mainly composed of α-synuclein (αSyn). Elevated levels of oxidative or nitrative stresses have been implicated in αSyn related toxicity. Phosphorylation of αSyn on serine 129 (S129) modulates autophagic clearance of inclusions and is prominently found in Lewy bodies. The neighboring tyrosine residues Y125, Y133 and Y136 are phosphorylation and nitration sites. Using a yeast model of PD, we found that Y133 is required for protective S129 phosphorylation and for S129-independent proteasome clearance. αSyn can be nitrated and form stable covalent dimers originating from covalent crosslinking of two tyrosine residues. Nitrated tyrosine residues, but not di-tyrosine-crosslinked dimers, contributed to αSyn cytotoxicity and aggregation. Analysis of tyrosine residues involved in nitration and crosslinking revealed that the C-terminus, rather than the N-terminus of αSyn, is modified by nitration and di-tyrosine formation. The nitration level of wild-type αSyn was higher compared to that of A30P mutant that is non-toxic in yeast. A30P formed more dimers than wild-type αSyn, suggesting that dimer formation represents a cellular detoxification pathway in yeast. Deletion of the yeast flavohemoglobin gene YHB1 resulted in an increase of cellular nitrative stress and cytotoxicity leading to enhanced aggregation of A30P αSyn. Yhb1 protected yeast from A30P-induced mitochondrial fragmentation and peroxynitrite-induced nitrative stress. Strikingly, overexpression of neuroglobin, the human homolog of YHB1, protected against αSyn inclusion formation in mammalian cells. In total, our data suggest that C-terminal Y133 plays a major role in αSyn aggregate clearance by supporting the protective S129 phosphorylation for autophagy and by promoting proteasome clearance. C-terminal tyrosine nitration increases pathogenicity and can only be partially detoxified by αSyn di-tyrosine dimers. Our findings uncover a complex interplay between S129 phosphorylation and C-terminal tyrosine modifications of αSyn that likely participates in PD pathology."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pgen.1006098"],["dc.identifier.pmid","27341336"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13384"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15831"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","1553-7404"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["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.firstpage","e1009407"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Wang, Dan"],["dc.contributor.author","Pätz, Christina"],["dc.contributor.author","Akkermann, Dagmar"],["dc.contributor.author","Lázaro, Diana F."],["dc.contributor.author","Galka, Dajana"],["dc.contributor.author","Kolog Gulko, Miriam"],["dc.contributor.author","Bohnsack, Markus T."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Bohnsack, Katherine E."],["dc.contributor.author","Outeiro, Tiago F."],["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.1009407"],["dc.identifier.pmid","33657088"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/82500"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/140"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.eissn","1553-7404"],["dc.relation.orgunit","Abteilung Molekulare Mikrobiologie & Genetik"],["dc.relation.workinggroup","RG K. Bohnsack (RNA Metabolism)"],["dc.rights","CC BY 4.0"],["dc.title","DEAD-box RNA helicase Dbp4/DDX10 is an enhancer of α-synuclein toxicity and oligomerization"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]