Braus, Gerhard H.

[["dc.bibliographiccitation.firstpage","909"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.lastpage","925"],["dc.bibliographiccitation.volume","405"],["dc.contributor.author","Herzog, Britta"],["dc.contributor.author","Streckfuss-Boemeke, Katrin"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:00:02Z"],["dc.date.available","2018-11-07T09:00:02Z"],["dc.date.issued","2011"],["dc.description.abstract","The basic zipper Gcn4 protein activates transcription in the yeast Saccharomyces cerevisiae in response to amino acid starvation. This includes numerous metabolic genes of amino acid or purine biosynthesis and the developmental cell-surface flocculin gene FLO11, which is required for diploid pseudohyphae formation and for adhesion upon nutrient starvation. We separated the metabolic from the developmental response by screening for GCN4 alleles that allow growth during amino acid starvation but are impaired in adhesion and are unable to form pseudohyphae. The identified Gcn4(L267S) variant carries an amino acid substitution in the third of the four conserved leucines of the zipper dimerization domain. This mutation abolished FLO11 expression and results in reduced but sufficient transcriptional activity for amino acid biosynthetic genes. The Leu267Ser substitution impairs Gcn4 homodimer formation and is a significantly more stable protein than the wild-type protein. A helix-breaker substitution in Leu253 results in a transcriptionally inactive but highly stable protein variant. This is due to a feedback circuit between transcriptional activity of Gcn4 and its own stability, which depends on the Gcn4-controlled cyclin PCL5. Gcn4(L253G) reduces the expression of Pcl5 and therefore reduces its own degradation. This self-controlled buffer system to restrict transcriptional activity results in a reciprocal correlation between Gcn4 transcriptional activity and protein stability. (C) 2010 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.jmb.2010.11.033"],["dc.identifier.isi","000286962300003"],["dc.identifier.pmid","21111745"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24051"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd- Elsevier Science Ltd"],["dc.relation.issn","0022-2836"],["dc.title","A Feedback Circuit between Transcriptional Activation and Self-Destruction of Gcn4 Separates Its Metabolic and Morphogenic Response in Diploid Yeasts"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","S91"],["dc.bibliographiccitation.journal","Medical Mycology"],["dc.bibliographiccitation.lastpage","S94"],["dc.bibliographiccitation.volume","44"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Sasse, Christoph"],["dc.contributor.author","Krappmann, Sven"],["dc.date.accessioned","2018-11-07T09:22:02Z"],["dc.date.available","2018-11-07T09:22:02Z"],["dc.date.issued","2006"],["dc.description.abstract","Supply of all amino acids required for translation is crucial for the synthesis of new proteins. Fungal amino acid biosynthesis has to be coordinated with amino acid uptake as well as protein degradation. A global regulator that connects amino acid biosynthesis and developmental programs is the transcription factor CpcA/Gcn4p. This transcriptional activator is conserved within the fungal kingdom and the cellular levels of this protein are carefully regulated. Deletion of the encoding cpcA gene in the opportunistic pathogen Aspergillus fumigatus results in impaired virulence in immuno-compromised mice, suggesting a role of the cross-pathway control system in fungal pathogenicity."],["dc.identifier.doi","10.1080/13693780600898029"],["dc.identifier.isi","000242601400017"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29246"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Taylor & Francis Ltd"],["dc.publisher.place","Abingdon"],["dc.relation.conference","2nd Advances against Aspergillosis Conference"],["dc.relation.eventlocation","Athens, GREECE"],["dc.relation.issn","1369-3786"],["dc.title","Amino acid acquisition, cross-pathway control, and virulence in Aspergillus"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","14"],["dc.bibliographiccitation.journal","Environmental and Experimental Botany"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Hoppenau, Clara E."],["dc.contributor.author","Tran, Van-Tuan"],["dc.contributor.author","Kusch, Harald"],["dc.contributor.author","Aßhauer, Kathrin P."],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-04-24T15:04:17Z"],["dc.date.available","2018-04-24T15:04:17Z"],["dc.date.issued","2014"],["dc.description.abstract","The vascular plant pathogen Verticillium dahliae colonizes the xylem fluid where only low nutrient concentrations are provided. Biosynthesis of the vitamin thiamine is connected to oxidative stress. The highly conserved VdThi4 protein is localized in fungal mitochondria and is required under vitamin B1 limiting conditions. Deletion of the corresponding VdTHI4 gene by Agrobacterium-mediated transformation resulted in strains which were impaired in growth on thiamine-free medium and could be rescued by additional vitamin supply or by complementation with the original gene after protoplastation. Furthermore, we show that VdThi4 increases fungal stress tolerance such as UV-damage or oxidative stress. The orthologous sti35 gene of Fusarium oxysporum, another vascular wilt fungus, was shown to be involved in stress response, however to be dispensable for pathogenicity on tomato. In contrast, VdTHI4 is required for fungal-induced tomato disease demonstrated by infection assays with a V. dahliae ΔVdTHI4 deletion strain which is still able to invade plants through the roots but is asymptomatic. Our results suggest remarkable differences between two vascular tomato pathogens where VdThi4 is required for pathogenicity of V. dahliae, whereas F. oxysporum still causes disease when the corresponding Sti35 protein is absent."],["dc.description.sponsorship","Federal Ministry of Education and Research (BMBF)"],["dc.description.sponsorship","Cluster of Excellence and DFG Research Center Nanoscale Microscopy and Molecular Physiology of the Brain"],["dc.identifier.doi","10.1016/j.envexpbot.2013.12.015"],["dc.identifier.other","http://www.sciencedirect.com/science/article/pii/S0098847213002268"],["dc.identifier.pii","S0098847213002268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13764"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.notes.status","zu prüfen"],["dc.relation.issn","0098-8472"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Verticillium dahliae VdTHI4, involved in thiazole biosynthesis, stress response and DNA repair functions, is required for vascular disease induction in tomato"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1125"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","1145"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Harting, Rebekka"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Laubinger, Karen"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T08:35:46Z"],["dc.date.available","2018-09-28T08:35:46Z"],["dc.date.issued","2013"],["dc.description.abstract","The role of the complex network of the ubiquitin-like modifier SumO in fungal development was analysed. SumO is not only required for sexual development but also for accurate induction and light stimulation of asexual development. The Aspergillus nidulans COMPASS complex including its subunits CclA and the methyltransferase SetA connects the SumO network to histone modification. SetA is required for correct positioning of aerial hyphae for conidiophore and asexual spore formation. Multicellular fungal development requires sumoylation and desumoylation. This includes the SumO processing enzyme UlpB, the E1 SumO activating enzyme AosA/UbaB, the E2 conjugation enzyme UbcN and UlpA as major SumO isopeptidase. Genetic suppression analysis suggests a connection between the genes for the Nedd8 isopeptidase DenA and the SumO isopeptidase UlpA and therefore a developmental interplay between neddylation and sumoylation in fungi. Biochemical evidence suggests an additional connection of the fungal SumO network with ubiquitination. Members of the cellular SumO network include histone modifiers, components of the transcription, RNA maturation and stress response machinery, or metabolic enzymes. Our data suggest that the SumO network controls specific temporal and spatial steps in fungal differentiation."],["dc.identifier.doi","10.1111/mmi.12421"],["dc.identifier.pmid","24279728"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15836"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1365-2958"],["dc.title","Interplay of the fungal sumoylation network for control of multicellular development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["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.issue","3"],["dc.bibliographiccitation.journal","mBio"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","de Assis, Leandro José"],["dc.contributor.author","Ulas, Mevlut"],["dc.contributor.author","Ries, Laure Nicolas Annick"],["dc.contributor.author","El Ramli, Nadia Ali Mohamed"],["dc.contributor.author","Sarikaya-Bayram, Ozlem"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Bayram, Ozgur"],["dc.contributor.author","Goldman, Gustavo Henrique"],["dc.contributor.editor","Yu, Jae-Hyuk"],["dc.contributor.editor","Bahn, Yong-Sun"],["dc.date.accessioned","2020-12-10T18:37:03Z"],["dc.date.available","2020-12-10T18:37:03Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1128/mBio.00840-18"],["dc.identifier.eissn","2150-7511"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76826"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Regulation of Aspergillus nidulans CreA-Mediated Catabolite Repression by the F-Box Proteins Fbx23 and Fbx47"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","21"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Fungal Genetics and Biology"],["dc.bibliographiccitation.lastpage","31"],["dc.bibliographiccitation.volume","32"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Draht, Oliver W."],["dc.contributor.author","Kubler, E."],["dc.contributor.author","Adler, K."],["dc.contributor.author","Hoffmann, Bernd"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:24:14Z"],["dc.date.available","2018-11-07T09:24:14Z"],["dc.date.issued","2001"],["dc.description.abstract","The hisHF gene of Aspergillus nidulans encodes imidazole-glycerole-phosphate (IGP) synthase, consisting of a glutamine amidotransferase and a cyclase domain. The enzyme catalyzes the fifth and sixth steps of histidine biosynthesis, which results in an intermediate of the amino acid and an additional intermediate of purine biosynthesis, An A. nidulans hisHF cDNA complemented a Saccharomyces cerevisiae his7 Delta strain and Escherichia coli hisH and hisF mutant strains, The genomic DNA encoding the hisHF gene was cloned and its sequence revealed two introns within the 1659-bp-long open reading frame. The transcription of the hisHF gene of A, nidulans is activated upon amino acid starvation, suggesting that hisHF is a target gene of cross pathway control, Adenine but not histidine, both end products of the biosynthetic pathways connected by the IGP synthase, represses hisHF transcription, In contrast to other organisms HISHF overproduction did not result in any developmental phenotype of the fungus in hyphal growth or the asexual life cycle, hisHF overexpression caused a significantly reduced osmotic tolerance and the inability to undergo the sexual life cycle leading to acleistothecial colonies. (C) 2001 Academic Press."],["dc.identifier.doi","10.1006/fgbi.2000.1244"],["dc.identifier.isi","000167960000003"],["dc.identifier.pmid","11277623"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29776"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","1096-0937"],["dc.relation.issn","1087-1845"],["dc.title","Regulation of hisHF transcription of Aspergillus nidulans by adenine and amino acid limitation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e0327321"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","mBio"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Horianopoulos, Linda C."],["dc.contributor.author","Lee, Christopher W. J."],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Hu, Guanggan"],["dc.contributor.author","Caza, Mélissa"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Kronstad, James W."],["dc.date.accessioned","2022-02-01T07:43:25Z"],["dc.date.available","2022-02-01T07:43:25Z"],["dc.date.issued","2021"],["dc.description.abstract","Histone chaperoning ensures genomic integrity during routine processes such as DNA replication and transcription as well as DNA repair upon damage. Here, we identify a nuclear J domain protein, Dnj4, in the fungal pathogen Cryptococcus neoformans and demonstrate that it interacts with histones 3 and 4, suggesting a role as a histone chaperone. In support of this idea, a dnj4Δ deletion mutant had elevated levels of DNA damage and was hypersensitive to DNA-damaging agents. The transcriptional response to DNA damage was also impaired in the dnj4Δ mutant. Genes related to DNA damage and iron homeostasis were upregulated in the wild-type strain in response to hydroxyurea treatment; however, their upregulation was either absent from or reduced in the dnj4Δ mutant. Accordingly, excess iron rescued the mutant's growth in response to DNA-damaging agents. Iron homeostasis is crucial for virulence in C. neoformans; however, Dnj4 was found to be dispensable for disease in a mouse model of cryptococcosis. Finally, we confirmed a conserved role for Dnj4 as a histone chaperone by expressing it in Saccharomyces cerevisiae and showing that it disrupted endogenous histone chaperoning. Altogether, this study highlights the importance of a JDP cochaperone in maintaining genome integrity in C. neoformans. IMPORTANCE DNA replication, gene expression, and genomic repair all require precise coordination of the many proteins that interact with DNA. This includes the histones as well as their chaperones. In this study, we show that a histone chaperone, Dnj4, is required for genome integrity and for the response to DNA damage. The gene encoding this protein in Cryptococcus neoformans lacks an ortholog in Saccharomyces cerevisiae; however, it is conserved in humans in which its ortholog is essential. Since it is not essential in C. neoformans, we were able to generate deletion mutants to characterize the roles of Dnj4. We also expressed Dnj4 in S. cerevisiae, in which it was able to bind S. cerevisiae histones and interfere with existing histone chaperoning machinery. Therefore, we show a conserved role for Dnj4 in histone chaperoning that suggests that C. neoformans is useful to better understand aspects of this important biological process."],["dc.identifier.doi","10.1128/mbio.03273-21"],["dc.identifier.pmid","34933457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/98735"],["dc.language.iso","en"],["dc.relation.eissn","2150-7511"],["dc.relation.orgunit","Institut für Mikrobiologie und Genetik"],["dc.title","A J Domain Protein Functions as a Histone Chaperone to Maintain Genome Integrity and the Response to DNA Damage in a Human Fungal Pathogen"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Brendel, Cornelia"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T08:51:10Z"],["dc.date.available","2018-11-07T08:51:10Z"],["dc.date.issued","2001"],["dc.format.extent","S86"],["dc.identifier.isi","000170442100137"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/21870"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","John Wiley & Sons Ltd"],["dc.publisher.place","W sussex"],["dc.relation.issn","0749-503X"],["dc.title","Different transcriptional activators regulating the same yeast gene act by different effects on nucleosomes of the promoter."],["dc.type","conference_abstract"],["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"]]