Valerius, Oliver

[["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","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","e1008996"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","de Assis, Leandro José"],["dc.contributor.author","Silva, Lilian Pereira"],["dc.contributor.author","Liu, Li"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Ries, Laure Nicolas Annick"],["dc.contributor.author","Goldman, Gustavo Henrique"],["dc.contributor.editor","Bahn, Yong-Sun"],["dc.date.accessioned","2021-04-14T08:23:54Z"],["dc.date.available","2021-04-14T08:23:54Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1371/journal.pgen.1008996"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/17631"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/81093"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-399"],["dc.relation.eissn","1553-7404"],["dc.title","The High Osmolarity Glycerol Mitogen-Activated Protein Kinase regulates glucose catabolite repression in filamentous fungi"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2137"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","The Plant Cell"],["dc.bibliographiccitation.lastpage","2160"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Kretzschmar, Franziska K."],["dc.contributor.author","Mengel, Laura A."],["dc.contributor.author","Müller, Anna O."],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Blersch, Katharina F."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Ischebeck, Till"],["dc.date.accessioned","2020-12-10T18:25:56Z"],["dc.date.available","2020-12-10T18:25:56Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1105/tpc.18.00276"],["dc.identifier.eissn","1532-298X"],["dc.identifier.issn","1040-4651"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75885"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","PUX10 Is a Lipid Droplet-Localized Scaffold Protein That Interacts with CELL DIVISION CYCLE48 and Is Involved in the Degradation of Lipid Droplet Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1054"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","1062"],["dc.bibliographiccitation.volume","272"],["dc.contributor.author","Angelov, A."],["dc.contributor.author","Futterer, O."],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Liebl, Wolfgang"],["dc.date.accessioned","2018-11-07T08:27:51Z"],["dc.date.available","2018-11-07T08:27:51Z"],["dc.date.issued","2005"],["dc.description.abstract","In Picrophilus torridus, a euryarchaeon that grows optimally at 60 degreesC and pH 0.7 and thus represents the most acidophilic thermophile known, glucose oxidation is the first proposed step of glucose catabolism via a nonphosphorylated variant of the Entner-Doudoroff pathway, as deduced from the recently completed genome sequence of this organism. The P. torridus gene for a glucose dehydrogenase was cloned and expressed in Escherichia coli, and the recombinant enzyme, GdhA, was purified and characterized. Based on its substrate and coenzyme specificity, physicochemical characteristics, and mobility during native PAGE, GdhA apparently resembles the main glucose dehydrogenase activity present in the crude extract of P. torridus DSM 9790 cells. The glucose dehydrogenase was partially purified from P. torridus cells and identified by MS to be identical with the recombinant GdhA. P. torridus GdhA preferred NADP(+) over NAD(+) as the coenzyme, but was nonspecific for the configuration at C-4 of the sugar substrate, oxidizing both glucose and its epimer galactose (K-m values 10.0 and 4.5 mm, respectively). Detection of a dual-specific glucose/galactose dehydrogenase points to the possibility that a 'promiscuous' Entner-Doudoroff pathway may operate in P. torridus, similar to the one recently postulated for the crenarchaeon Sulfolobus solfataricus. Based on Zn2+ supplementation and chelation experiments, the P. torridus GdhA appears to contain structurally important zinc, and conserved metal-binding residues suggest that the enzyme also contains a zinc ion near the catalytic site, similar to the glucose dehydrogenase enzymes from yeast and Thermoplasma acidophilum. Strikingly, NADPH, one of the products of the GdhA reaction, is unstable under the conditions thought to prevail in Picrophilus cells, which have been reported to maintain the lowest cytoplasmic pH known (pH 4.6). At the optimum growth temperature for P. torridus, 60 degreesC, the half-life of NADPH at pH 4.6 was merely 2.4 min, and only 1.7 min at 65 degreesC (maximum growth temperature). This finding suggests a rapid turnover of NADPH in Picrophilus."],["dc.identifier.doi","10.1111/j.1742-4658.2004.04539.x"],["dc.identifier.isi","000227359500016"],["dc.identifier.pmid","15691337"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16292"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing Ltd"],["dc.relation.issn","1742-464X"],["dc.title","Properties of the recombinant glucose/galactose dehydrogenase from the extreme thermoacidophile, Picrophilus torridus"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","314"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Current Genetics"],["dc.bibliographiccitation.lastpage","322"],["dc.bibliographiccitation.volume","38"],["dc.contributor.author","Busch, S."],["dc.contributor.author","Hoffmann, Bernd"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Starke, K."],["dc.contributor.author","Duvel, K."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:30:50Z"],["dc.date.available","2018-11-07T09:30:50Z"],["dc.date.issued","2001"],["dc.description.abstract","The hisB gene of the filamentous fungus Aspergillus nidulans encodes imidazole glycerol-phosphate dehydratase (E.C. 4.2.1.19), which catalyses the seventh enzymatic step in histidine biosynthesis. The gene was isolated and its deduced peptide sequence of 247 amino acids showed up to 54% identity with the IGPD enzymes of organisms comprising all three kingdoms. Expression of hisB cDNA in a Saccharomyces cerevisiae his3 Delta mutant strain functionally complemented the growth phenotype under histidine limitation. Addition of histidine did not affect hisB mRNA levels A. nidulans wild-type cells. Histidine starvation conditions increased the hisB transcript level four-fold, suggesting regulation by a cross-pathway regulatory network. Deletion of the complete hisB open reading frame in A. nidulans strain A234 resulted in histidine auxotrophy. Additionally, hisB deletion strains were blocked from sexual fruiting body formation on medium containing low concentrations of histidine. This developmental phenotype of the hisB deletion mutant strain correlated with the induction of the cross-pathway control system."],["dc.identifier.doi","10.1007/s002940000171"],["dc.identifier.isi","000166406900003"],["dc.identifier.pmid","11270573"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31406"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","1432-0983"],["dc.relation.issn","0172-8083"],["dc.title","Regulation of the Aspergillus nidulans hisB gene by histidine starvation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1326"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Plant Physiology"],["dc.bibliographiccitation.lastpage","1345"],["dc.bibliographiccitation.volume","182"],["dc.contributor.author","Kretzschmar, Franziska K."],["dc.contributor.author","Doner, Nathan M."],["dc.contributor.author","Krawczyk, Hannah E."],["dc.contributor.author","Scholz, Patricia"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Mullen, Robert T."],["dc.contributor.author","Ischebeck, Till"],["dc.date.accessioned","2020-12-10T18:25:55Z"],["dc.date.available","2020-12-10T18:25:55Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.1104/pp.19.01255"],["dc.identifier.eissn","1532-2548"],["dc.identifier.issn","0032-0889"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75878"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Identification of Low-Abundance Lipid Droplet Proteins in Seeds and Seedlings"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["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"]]