Valerius, Oliver

[["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.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","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.firstpage","682"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","Journal of Fungi"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Groth, Anika"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Herzog, Britta"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.date.accessioned","2021-12-01T09:24:06Z"],["dc.date.available","2021-12-01T09:24:06Z"],["dc.date.issued","2021"],["dc.description.abstract","In the filamentous fungus Sordaria macrospora (Sm), the STRIPAK complex is required for vegetative growth, fruiting-body development and hyphal fusion. The SmSTRIPAK core consists of the striatin homolog PRO11, the scaffolding subunit of phosphatase PP2A, SmPP2AA, and its catalytic subunit SmPP2Ac1. Among other STRIPAK proteins, the recently identified coiled-coil protein SCI1 was demonstrated to co-localize around the nucleus. Pulldown experiments with SCI identified the transmembrane nucleoporin (TM Nup) SmPOM33 as a potential nuclear-anchor of SmSTRIPAK. Localization studies revealed that SmPOM33 partially localizes to the nuclear envelope (NE), but mainly to the endoplasmic reticulum (ER). We succeeded to generate a Δpom33 deletion mutant by homologous recombination in a new S. macrospora Δku80 recipient strain, which is defective in non-homologous end joining. Deletion of Smpom33 did neither impair vegetative growth nor sexual development. In pulldown experiments of SmPOM33 followed by LC/MS analysis, ER-membrane proteins involved in ER morphology, protein translocation, glycosylation, sterol biosynthesis and Ca2+-transport were significantly enriched. Data are available via ProteomeXchange with identifier PXD026253. Although no SmSTRIPAK components were identified as putative interaction partners, it cannot be excluded that SmPOM33 is involved in temporarily anchoring the SmSTRIPAK to the NE or other sites in the cell."],["dc.description.abstract","In the filamentous fungus Sordaria macrospora (Sm), the STRIPAK complex is required for vegetative growth, fruiting-body development and hyphal fusion. The SmSTRIPAK core consists of the striatin homolog PRO11, the scaffolding subunit of phosphatase PP2A, SmPP2AA, and its catalytic subunit SmPP2Ac1. Among other STRIPAK proteins, the recently identified coiled-coil protein SCI1 was demonstrated to co-localize around the nucleus. Pulldown experiments with SCI identified the transmembrane nucleoporin (TM Nup) SmPOM33 as a potential nuclear-anchor of SmSTRIPAK. Localization studies revealed that SmPOM33 partially localizes to the nuclear envelope (NE), but mainly to the endoplasmic reticulum (ER). We succeeded to generate a Δpom33 deletion mutant by homologous recombination in a new S. macrospora Δku80 recipient strain, which is defective in non-homologous end joining. Deletion of Smpom33 did neither impair vegetative growth nor sexual development. In pulldown experiments of SmPOM33 followed by LC/MS analysis, ER-membrane proteins involved in ER morphology, protein translocation, glycosylation, sterol biosynthesis and Ca2+-transport were significantly enriched. Data are available via ProteomeXchange with identifier PXD026253. Although no SmSTRIPAK components were identified as putative interaction partners, it cannot be excluded that SmPOM33 is involved in temporarily anchoring the SmSTRIPAK to the NE or other sites in the cell."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/jof7090682"],["dc.identifier.pii","jof7090682"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94847"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation.eissn","2309-608X"],["dc.relation.orgunit","Institut für Mikrobiologie und Genetik"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Analysis of the Putative Nucleoporin POM33 in the Filamentous Fungus Sordaria macrospora"],["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","1337"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","1353"],["dc.bibliographiccitation.volume","17"],["dc.contributor.author","Baade, Imke"],["dc.contributor.author","Spillner, Christiane"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Kehlenbach, Ralph H."],["dc.date.accessioned","2020-12-10T18:12:59Z"],["dc.date.available","2020-12-10T18:12:59Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1074/mcp.RA118.000623"],["dc.identifier.eissn","1535-9484"],["dc.identifier.issn","1535-9476"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/74553"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Extensive Identification and In-depth Validation of Importin 13 Cargoes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","tpj.15802"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.contributor.author","Kasper, Karl"],["dc.contributor.author","Abreu, Ilka N."],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Zienkiewicz, Krzysztof"],["dc.contributor.author","Herrfurth, Cornelia"],["dc.contributor.author","Ischebeck, Till"],["dc.contributor.author","Janz, Dennis"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Polle, Andrea"],["dc.date.accessioned","2022-06-01T09:39:32Z"],["dc.date.available","2022-06-01T09:39:32Z"],["dc.date.issued","2022"],["dc.identifier.doi","10.1111/tpj.15802"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/108504"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-572"],["dc.relation.eissn","1365-313X"],["dc.relation.issn","0960-7412"],["dc.title","Multi‐omics analysis of xylem sap uncovers dynamic modulation of poplar defenses by ammonium and nitrate"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","87"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Molecular & Cellular Proteomics"],["dc.bibliographiccitation.lastpage","105"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Rachfall, Nicole"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Bandau, Susanne"],["dc.contributor.author","Smolinski, Nadine"],["dc.contributor.author","Ehrenreich, Armin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:30:39Z"],["dc.date.available","2018-11-07T09:30:39Z"],["dc.date.issued","2013"],["dc.description.abstract","RACK1/Asc1p and its essential orthologues in higher eukaryotes, such as RACK1 in metazoa, are involved in several distinct cellular signaling processes. The implications of a total deletion have never been assessed in a comprehensive manner. This study reveals the major cellular processes affected in a Saccharomyces cerevisiae Delta asc1 deletion background via de novo proteome and transcriptome analysis, as well as subsequent phenotypical characterizations. The deletion of ASC1 reduces iron uptake and causes nitrosative stress, both known indicators for hypoxia, which manifests in a shift of energy metabolism from respiration to fermentation in the Delta asc1 strain. Asc1p further impacts cellular metabolism through its regulative role in the MAP kinase signal transduction pathways of invasive/filamentous growth and cell wall integrity. In the Delta asc1 mutant strain, aberrations from the expected cellular response, mediated by these pathways, can be observed and are linked to changes in protein abundances of pathway-targeted transcription factors. Evidence of the translational regulation of such transcription factors suggests that ribosomal Asc1p is involved in signal transduction pathways and controls the biosynthesis of the respective final transcriptional regulators. Molecular & Cellular Proteomics 12: 10.1074/mcp.M112.017277, 87-105, 2013."],["dc.identifier.doi","10.1074/mcp.M112.017277"],["dc.identifier.isi","000313557600007"],["dc.identifier.pmid","23071099"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31359"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Biochemistry Molecular Biology Inc"],["dc.relation.issn","1535-9476"],["dc.title","RACK1/Asc1p, a Ribosomal Node in Cellular Signaling"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1192"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Beißbarth, Tim"],["dc.contributor.author","Bohrer, Rainer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Asif, Abdul R."],["dc.contributor.author","Dihazi, Hassan"],["dc.contributor.author","Majcherczyk, Andrzej"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Lenz, Christof"],["dc.date.accessioned","2020-04-02T10:32:12Z"],["dc.date.available","2020-04-02T10:32:12Z"],["dc.date.issued","2019"],["dc.description.abstract","Mass spectrometry-based proteomics methods are finding increasing use in structural biology research. Beyond simple interaction networks, information about stable protein-protein complexes or spatially proximal proteins helps to elucidate the biological functions of proteins in a wider cellular context. To shed light on new developments in this field, the Göttingen Proteomics Forum organized a one-day symposium focused on complexome profiling and proximity labeling, two emerging technologies that are gaining significant attention in biomolecular research. The symposium was held in Göttingen, Germany on 23 May, 2019, as part of a series of regular symposia organized by the Göttingen Proteomics Forum."],["dc.identifier.doi","10.3390/cells8101192"],["dc.identifier.pmid","31581721"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16914"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/63512"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/95"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.publisher","MDPI"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z02: Massenspektrometrie-basierte Proteomanalyse"],["dc.relation.conference","Seventh Symposium of the Göttingen Proteomics Forum"],["dc.relation.eissn","2073-4409"],["dc.relation.eventlocation","Göttingen"],["dc.relation.eventstart","2019-05-23"],["dc.relation.issn","2073-4409"],["dc.relation.orgunit","Gesellschaft für wissenschaftliche Datenverarbeitung"],["dc.relation.workinggroup","RG Urlaub (Bioanalytische Massenspektrometrie)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mapping Cellular Microenvironments: Proximity Labeling and Complexome Profiling"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","796"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","812"],["dc.bibliographiccitation.volume","90"],["dc.contributor.author","Dettmann, Anne"],["dc.contributor.author","Heilig, Yvonne"],["dc.contributor.author","Ludwig, Sarah"],["dc.contributor.author","Schmitt, Kerstin"],["dc.contributor.author","Illgen, Julia"],["dc.contributor.author","Fleissner, Andre"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Seiler, Stephan"],["dc.date.accessioned","2018-11-07T09:17:45Z"],["dc.date.available","2018-11-07T09:17:45Z"],["dc.date.issued","2013"],["dc.description.abstract","Intercellular communication and somatic cell fusion are important for fungal colony establishment, multicellular differentiation and have been associated with host colonization and virulence of pathogenic species. By a combination of genetic, biochemical and live cell imaging techniques, we characterized the Neurospora crassaSTRIPAK complex that is essential for self-signalling and consists of the six proteins HAM-2/STRIP, HAM-3/striatin, HAM-4/SLMAP, MOB-3/phocein, PPG-1/PP2A-C and PP2A-A. We describe that the core STRIPAK components HAM-2 and HAM-3 are central for the assembly of the complex at the nuclear envelope, while the phosphatase PPG-1 only transiently associates with this central subcomplex. Our data connect the STRIPAK complex with two MAP kinase pathways: (i) nuclear accumulation of the cell wall integrity MAP kinase MAK-1 depends on the functional integrity of the STRIPAK complex at the nuclear envelope, and (ii) phosphorylation of MOB-3 by the MAP kinase MAK-2 impacts the nuclear accumulation of MAK-1. In summary, these data support a model, in which MAK-2-dependent phosphorylation of MOB-3 is part of a MAK-1 import mechanism. Although self-communication remained intact in the absence of nuclear MAK-1 accumulation, supporting the presence of multiple mechanisms that co-ordinate robust intercellular communication, proper fruiting body morphology was dependent on the MAK-2-phosphorylated N-terminus of MOB-3."],["dc.identifier.doi","10.1111/mmi.12399"],["dc.identifier.isi","000330108000009"],["dc.identifier.pmid","24028079"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28245"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1365-2958"],["dc.relation.issn","0950-382X"],["dc.title","HAM-2 and HAM-3 are central for the assembly of the Neurospora STRIPAK complex at the nuclear envelope and regulate nuclear accumulation of the MAP kinase MAK-1 in a MAK-2-dependent manner"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]