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Pöggeler, Stefanie
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Pöggeler, Stefanie
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Pöggeler, Stefanie
Alternative Name
Pöggeler, S.
Poeggeler, Stefanie
Poeggeler, S.
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2022Journal Article [["dc.bibliographiccitation.firstpage","407"],["dc.bibliographiccitation.issue","3-4"],["dc.bibliographiccitation.journal","Current Genetics"],["dc.bibliographiccitation.lastpage","427"],["dc.bibliographiccitation.volume","68"],["dc.contributor.author","Groth, Anika"],["dc.contributor.author","Ahlmann, Svenja"],["dc.contributor.author","Werner, Antonia"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.date.accessioned","2022-09-01T09:51:28Z"],["dc.date.available","2022-09-01T09:51:28Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract\n \n The multiprotein Fab1p/PIKfyve-complex regulating the abundance of the phospholipid phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P\n 2\n ) is highly conserved among eukaryotes. In yeast/mammals, it is composed of the phosphatidylinositol 3-phosphate 5-kinase Fab1p/PIKfyve, the PtdIns(3,5)P\n 2\n phosphatase Fig4p/Sac3 and the scaffolding subunit Vac14p/ArPIKfyve. The complex is located to vacuolar membranes in yeast and to endosomal membranes in mammals, where it controls the synthesis and turnover of PtdIns(3,5)P\n 2\n . In this study, we analyzed the role and function of the Fab1p/PIKfyve-complex scaffold protein SmVAC14 in the filamentous ascomycete\n Sordaria macrospora\n (Sm). We generated the\n Smvac14\n deletion strain ∆vac14 and performed phenotypic analysis of the mutant. Furthermore, we conducted fluorescence microscopic localization studies of fluorescently labeled SmVAC14 with vacuolar and late endosomal marker proteins. Our results revealed that SmVAC14 is important for maintaining vacuolar size and appearance as well as proper sexual development in\n S. macrospora\n . In addition, SmVAC14 plays an important role in starvation stress response. Accordingly, our results propose that the turnover of PtdIns(3,5)P\n 2\n is of great significance for developmental processes in filamentous fungi."],["dc.description.sponsorship"," Deutsche Forschungsgemeinschaft http://dx.doi.org/10.13039/501100001659"],["dc.description.sponsorship"," Georg-August-Universität Göttingen http://dx.doi.org/10.13039/501100003385"],["dc.identifier.doi","10.1007/s00294-022-01244-0"],["dc.identifier.pii","1244"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/113972"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-597"],["dc.relation.eissn","1432-0983"],["dc.relation.issn","0172-8083"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","The vacuolar morphology protein VAC14 plays an important role in sexual development in the filamentous ascomycete Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2013Journal Article [["dc.bibliographiccitation.artnumber","e1003820"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Traeger, Stefanie"],["dc.contributor.author","Altegoer, Florian"],["dc.contributor.author","Freitag, Michael"],["dc.contributor.author","Gabaldon, Toni"],["dc.contributor.author","Kempken, Frank"],["dc.contributor.author","Kumar, Abhishek"],["dc.contributor.author","Marcet-Houben, Marina"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.contributor.author","Stajich, Jason E."],["dc.contributor.author","Nowrousian, Minou"],["dc.date.accessioned","2018-11-07T09:20:30Z"],["dc.date.available","2018-11-07T09:20:30Z"],["dc.date.issued","2013"],["dc.description.abstract","Fungi are a large group of eukaryotes found in nearly all ecosystems. More than 250 fungal genomes have already been sequenced, greatly improving our understanding of fungal evolution, physiology, and development. However, for the Pezizomycetes, an early-diverging lineage of filamentous ascomycetes, there is so far only one genome available, namely that of the black truffle, Tuber melanosporum, a mycorrhizal species with unusual subterranean fruiting bodies. To help close the sequence gap among basal filamentous ascomycetes, and to allow conclusions about the evolution of fungal development, we sequenced the genome and assayed transcriptomes during development of Pyronema confluens, a saprobic Pezizomycete with a typical apothecium as fruiting body. With a size of 50 Mb and similar to 13,400 protein-coding genes, the genome is more characteristic of higher filamentous ascomycetes than the large, repeat-rich truffle genome; however, some typical features are different in the P. confluens lineage, e.g. the genomic environment of the mating type genes that is conserved in higher filamentous ascomycetes, but only partly conserved in P. confluens. On the other hand, P. confluens has a full complement of fungal photoreceptors, and expression studies indicate that light perception might be similar to distantly related ascomycetes and, thus, represent a basic feature of filamentous ascomycetes. Analysis of spliced RNA-seq sequence reads allowed the detection of natural antisense transcripts for 281 genes. The P. confluens genome contains an unusually high number of predicted orphan genes, many of which are upregulated during sexual development, consistent with the idea of rapid evolution of sex-associated genes. Comparative transcriptomics identified the transcription factor gene pro44 that is upregulated during development in P. confluens and the Sordariomycete Sordaria macrospora. The P. confluens pro44 gene (PCON_06721) was used to complement the S. macrospora pro44 deletion mutant, showing functional conservation of this developmental regulator."],["dc.identifier.doi","10.1371/journal.pgen.1003820"],["dc.identifier.isi","000325076600074"],["dc.identifier.pmid","24068976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9290"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28893"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","The Genome and Development-Dependent Transcriptomes of Pyronema confluens: A Window into Fungal Evolution"],["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"]]Details DOI PMID PMC WOS2016Journal Article [["dc.bibliographiccitation.artnumber","e0157960"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Werner, Antonia"],["dc.contributor.author","Herzog, Britta"],["dc.contributor.author","Frey, Stefan"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T10:12:44Z"],["dc.date.available","2018-11-07T10:12:44Z"],["dc.date.issued","2016"],["dc.description.abstract","In filamentous fungi, autophagy functions as a catabolic mechanism to overcome starvation and to control diverse developmental processes under normal nutritional conditions. Autophagy involves the formation of double-membrane vesicles, termed autophagosomes that engulf cellular components and bring about their degradation via fusion with vacuoles. Two ubiquitin-like (UBL) conjugation systems are essential for the expansion of the autophagosomal membrane: the UBL protein ATG8 is conjugated to the lipid phosphatidylethanolamine and the UBL protein ATG12 is coupled to ATG5. We recently showed that in the homothallic ascomycete Sordaria macrospora autophagy-related genes encoding components of the conjugation systems are required for fruiting-body development and/or are essential for viability. In the present work, we cloned and characterized the S. macrospora (Sm)atg12 gene. Two-hybrid analysis revealed that SmATG12 can interact with SmATG7 and SmATG3. To examine its role in S. macrospora, we replaced the open reading frame of Smatg12 with a hygromycin resistance cassette and generated a homokaryotic Delta Smatg12 knockout strain, which displayed slower vegetative growth under nutrient starvation conditions and was unable to form fruiting bodies. In the hyphae of S. macrospora EGFP-labeled SmATG12 was detected in the cytoplasm and as punctate structures presumed to be phagophores or phagophore assembly sites. Delivery of EGFP-labelled SmATG8 to the vacuole was entirely dependent on SmATG12."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2016"],["dc.identifier.doi","10.1371/journal.pone.0157960"],["dc.identifier.isi","000378029800144"],["dc.identifier.pmid","27309377"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13387"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40297"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Autophagy-Associated Protein SmATG12 Is Required for Fruiting-Body Formation in the Filamentous Ascomycete Sordaria macrospora"],["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"]]Details DOI PMID PMC WOS2020Journal Article [["dc.bibliographiccitation.firstpage","93"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Metabolites"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Vullo, Daniela"],["dc.contributor.author","Lehneck, Ronny"],["dc.contributor.author","Donald, William A."],["dc.contributor.author","Pöggeler, Stefanie"],["dc.contributor.author","Supuran, Claudiu T."],["dc.date.accessioned","2020-12-10T18:47:15Z"],["dc.date.available","2020-12-10T18:47:15Z"],["dc.date.issued","2020"],["dc.identifier.doi","10.3390/metabo10030093"],["dc.identifier.eissn","2218-1989"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/78697"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.publisher","MDPI"],["dc.relation.eissn","2218-1989"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Anion Inhibition Studies of the β-Class Carbonic Anhydrase CAS3 from the Filamentous Ascomycete Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]Details DOI2014Journal Article Research Paper [["dc.bibliographiccitation.firstpage","1759"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","1772"],["dc.bibliographiccitation.volume","281"],["dc.contributor.author","Lehneck, Ronny"],["dc.contributor.author","Neumann, Piotr"],["dc.contributor.author","Vullo, Daniela"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Supuran, Claudiu T."],["dc.contributor.author","Ficner, Ralf"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.date.accessioned","2017-09-07T11:46:22Z"],["dc.date.available","2017-09-07T11:46:22Z"],["dc.date.issued","2014"],["dc.description.abstract","Carbonic anhydrases (CAs) are metalloenzymes catalyzing the reversible hydration of carbon dioxide to bicarbonate (hydrogen carbonate) and protons. CAs have been identified in archaea, bacteria and eukaryotes and can be classified into five groups (, , , , ) that are unrelated in sequence and structure. The fungal -class has only recently attracted attention. In the present study, we investigated the structure and function of the plant-like -CA proteins CAS1 and CAS2 from the filamentous ascomycete Sordariamacrospora. We demonstrated that both proteins can substitute for the Saccharomycescerevisiae -CA Nce103 and exhibit an invitro CO2 hydration activity (k(cat)/K-m of CAS1:1.30x10(6)m(-1)s(-1); CAS2:1.21x10(6)m(-1)s(-1)). To further investigate the structural properties of CAS1 and CAS2, we determined their crystal structures to a resolution of 2.7 angstrom and 1.8 angstrom, respectively. The oligomeric state of both proteins is tetrameric. With the exception of the active site composition, no further major differences have been found. In both enzymes, the Zn2+-ion is tetrahedrally coordinated; in CAS1 by Cys45, His101 and Cys104 and a water molecule and in CAS2 by the side chains of four residues (Cys56, His112, Cys115 and Asp58). Both CAs are only weakly inhibited by anions, making them good candidates for industrial applications. Structured digital abstract andby() DatabaseStructural data have been deposited in the Protein Data Bank database under accession numbers for CAS1 and for CAS2."],["dc.identifier.doi","10.1111/febs.12738"],["dc.identifier.gro","3142157"],["dc.identifier.isi","000333676000005"],["dc.identifier.pmid","24506675"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5166"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1742-4658"],["dc.relation.issn","1742-464X"],["dc.title","Crystal structures of two tetrameric β‐carbonic anhydrases from the filamentous ascomycete Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2021Journal Article Research Paper [["dc.bibliographiccitation.firstpage","580"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Journal of Fungi"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Groth, Anika"],["dc.contributor.author","Schunke, Carolin"],["dc.contributor.author","Reschka, Eva"],["dc.contributor.author","Pöggeler, Stefanie"],["dc.contributor.author","Nordzieke, Daniela"],["dc.date.accessioned","2021-08-12T07:46:01Z"],["dc.date.available","2021-08-12T07:46:01Z"],["dc.date.issued","2021"],["dc.description.abstract","Polar growth is a key characteristic of all filamentous fungi. It allows these eukaryotes to not only effectively explore organic matter but also interact within its own colony, mating partners, and hosts. Therefore, a detailed understanding of the dynamics in polar growth establishment and maintenance is crucial for several fields of fungal research. We developed a new marker protein, the actin-related protein 1 (Arp1) fused to red and green fluorescent proteins, which allows for the tracking of polar axis establishment and active hyphal growth in microscopy approaches. To exclude a probable redundancy with known polarity markers, we compared the localizations of the Spitzenkörper (SPK) and Arp1 using an FM4-64 staining approach. As we show in applications with the coprophilous fungus Sordaria macrospora and the hemibiotrophic plant pathogen Colletotrichum graminicola, the monitoring of Arp1 can be used for detailed studies of hyphal growth dynamics and ascospore germination, the interpretation of chemotropic growth processes, and the tracking of elongating penetration pegs into plant material. Since the Arp1 marker showed the same dynamics in both fungi tested, we believe this marker can be broadly applied in fungal research to study the manifold polar growth processes determining fungal life."],["dc.description.abstract","Polar growth is a key characteristic of all filamentous fungi. It allows these eukaryotes to not only effectively explore organic matter but also interact within its own colony, mating partners, and hosts. Therefore, a detailed understanding of the dynamics in polar growth establishment and maintenance is crucial for several fields of fungal research. We developed a new marker protein, the actin-related protein 1 (Arp1) fused to red and green fluorescent proteins, which allows for the tracking of polar axis establishment and active hyphal growth in microscopy approaches. To exclude a probable redundancy with known polarity markers, we compared the localizations of the Spitzenkörper (SPK) and Arp1 using an FM4-64 staining approach. As we show in applications with the coprophilous fungus Sordaria macrospora and the hemibiotrophic plant pathogen Colletotrichum graminicola, the monitoring of Arp1 can be used for detailed studies of hyphal growth dynamics and ascospore germination, the interpretation of chemotropic growth processes, and the tracking of elongating penetration pegs into plant material. Since the Arp1 marker showed the same dynamics in both fungi tested, we believe this marker can be broadly applied in fungal research to study the manifold polar growth processes determining fungal life."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (DFG)"],["dc.description.sponsorship","Open-Access-Publikationsfonds 2021"],["dc.identifier.doi","10.3390/jof7070580"],["dc.identifier.pii","jof7070580"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/88597"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-448"],["dc.relation.eissn","2309-608X"],["dc.relation.orgunit","Abteilung Genetik eukaryotischer Mikroorganismen"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Tracking Fungal Growth: Establishment of Arp1 as a Marker for Polarity Establishment and Active Hyphal Growth in Filamentous Ascomycetes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]Details DOI2015Journal Article [["dc.bibliographiccitation.firstpage","676"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","697"],["dc.bibliographiccitation.volume","97"],["dc.contributor.author","Frey, Stefan"],["dc.contributor.author","Lahmann, Yasmine"],["dc.contributor.author","Hartmann, Thomas"],["dc.contributor.author","Seiler, Stephan"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T09:53:48Z"],["dc.date.available","2018-11-07T09:53:48Z"],["dc.date.issued","2015"],["dc.description.abstract","The striatin interacting phosphatase and kinase (STRIPAK) complex, which is composed of striatin, protein phosphatase PP2A and kinases, is required for fruiting-body development and cell fusion in the filamentous ascomycete Sordaria macrospora. Here, we report on the interplay of the glycosylphosphatidylinositol (GPI)-anchored protein SmGPI1 with the kinase activator SmMOB3, a core component of human and fungal STRIPAK complexes. SmGPI1 is conserved among filamentous ascomycetes and was first identified in a yeast two-hybrid screen using SmMOB3 as bait. The physical interaction of SmMOB3 and SmGPI1 was verified by co-immunoprecipitation. In vivo localization and differential centrifugation revealed that SmGPI1 is predominantly secreted and attached to the cell wall but is also associated with mitochondria and appears to be a dual-targeted protein. Deletion of Smgpi1 led to an increased number of fruiting bodies that were normally shaped but reduced in size. In addition, Smmob3 and Smgpi1 genetically interact. In the sterile Delta Smmob3 background deletion of Smgpi1 restores fertility, vegetative growth as well as hyphal-fusion defects. The suppression effect was specific for the Delta Smmob3 mutant as deletion of Smgpi1 in other STRIPAK mutants does not restore fertility."],["dc.identifier.doi","10.1111/mmi.13054"],["dc.identifier.isi","000359677500007"],["dc.identifier.pmid","25989468"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/36406"],["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","Deletion of Smgpi1 encoding a GPI-anchored protein suppresses sterility of the STRIPAK mutant Smmob3 in the filamentous ascomycete Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2021Journal Article Research Paper [["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"]]Details DOI2009Journal Article [["dc.bibliographiccitation.artnumber","e5177"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T08:30:47Z"],["dc.date.available","2018-11-07T08:30:47Z"],["dc.date.issued","2009"],["dc.description.abstract","Carbon dioxide (CO(2)) is among the most important gases for all organisms. Its reversible interconversion to bicarbonate (HCO(3)(-)) reaches equilibrium spontaneously, but slowly, and can be accelerated by a ubiquitous group of enzymes called carbonic anhydrases (CAs). These enzymes are grouped by their distinct structural features into alpha-, beta-, gamma-, delta-and zeta-classes. While physiological functions of mammalian, prokaryotic, plant and algal CAs have been extensively studied over the past years, the role of beta-CAs in yeasts and the human pathogen Cryptococcus neoformans has been elucidated only recently, and the function of CAs in multicellular filamentous ascomycetes is mostly unknown. To assess the role of CAs in the development of filamentous ascomycetes, the function of three genes, cas1, cas2 and cas3 (carbonic anhydrase of Sordaria) encoding beta-class carbonic anhydrases was characterized in the filamentous ascomycetous fungus Sordaria macrospora. Fluorescence microscopy was used to determine the localization of GFP- and DsRED-tagged CAs. While CAS1 and CAS3 are cytoplasmic enzymes, CAS2 is localized to the mitochondria. To assess the function of the three isoenzymes, we generated knock-out strains for all three cas genes (Delta cas1, Delta cas2, and Delta cas3) as well as all combinations of double mutants. No effect on vegetative growth, fruiting-body and ascospore development was seen in the single mutant strains lacking cas1 or cas3, while single mutant Delta cas2 was affected in vegetative growth, fruiting-body development and ascospore germination, and the double mutant strain Delta cas1/2 was completely sterile. Defects caused by the lack of cas2 could be partially complemented by elevated CO(2) levels or overexpression of cas1, cas3, or a non-mitochondrial cas2 variant. The results suggest that CAs are required for sexual reproduction in filamentous ascomycetes and that the multiplicity of isoforms results in redundancy of specific and non-specific functions."],["dc.identifier.doi","10.1371/journal.pone.0005177"],["dc.identifier.isi","000265509900007"],["dc.identifier.pmid","19365544"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8275"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16974"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","beta-Carbonic Anhydrases Play a Role in Fruiting Body Development and Ascospore Germination in the Filamentous Fungus Sordaria macrospora"],["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"]]Details DOI PMID PMC WOS2015Journal Article [["dc.bibliographiccitation.firstpage","465"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Genome Biology and Evolution"],["dc.bibliographiccitation.lastpage","480"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Karlsson, Magnus"],["dc.contributor.author","Durling, Mikael Brandstrom"],["dc.contributor.author","Choi, Jaeyoung"],["dc.contributor.author","Kosawang, Chatchai"],["dc.contributor.author","Lackner, Gerald"],["dc.contributor.author","Tzelepis, Georgios D."],["dc.contributor.author","Nygren, Kristiina"],["dc.contributor.author","Dubey, Mukesh K."],["dc.contributor.author","Kamou, Nathalie"],["dc.contributor.author","Levasseur, Anthony"],["dc.contributor.author","Zapparata, Antonio"],["dc.contributor.author","Wang, J."],["dc.contributor.author","Amby, Daniel Buchvaldt"],["dc.contributor.author","Jensen, Birgit"],["dc.contributor.author","Sarrocco, Sabrina"],["dc.contributor.author","Panteris, Emmanuel"],["dc.contributor.author","Lagopodi, Anastasia L."],["dc.contributor.author","Poeggeler, Stefanie"],["dc.contributor.author","Vannacci, Giovanni"],["dc.contributor.author","Collinge, David B."],["dc.contributor.author","Hoffmeister, Dirk"],["dc.contributor.author","Henrissat, Bernard"],["dc.contributor.author","Lee, Yong-Hwan"],["dc.contributor.author","Jensen, Dan Funck"],["dc.date.accessioned","2018-11-07T10:01:16Z"],["dc.date.available","2018-11-07T10:01:16Z"],["dc.date.issued","2015"],["dc.description.abstract","Clonostachys rosea is a mycoparasitic fungus that can control several important plant diseases. Here, we report on the genome sequencing of C. rosea and a comparative genome analysis, in order to resolve the phylogenetic placement of C. rosea and to study the evolution of mycoparasitism as a fungal lifestyle. The genome of C. rosea is estimated to 58.3 Mb, and contains 14,268 predicted genes. A phylogenomic analysis shows that C. Tosco clusters as sister taxon to plant pathogenic Fusarium species, with mycoparasitic/saprotrophic Tfichoderma species in an ancestral position. A comparative analysis of gene family evolution reveals several distinct differences between the included mycoparasites. Clonostachys rosea contains significantly more ATP-binding cassette (ABC) transporters, polyketide synthases, cytochrome P450 monooxygenases, pectin lyases, glucose-methanol-choline oxidoreductases, and lytic polysaccharide monooxygenases compared with other fungi in the Hypocreales. Interestingly, the increase of ABC transporter gene number in C. rosea is associated with phylogenetic subgroups B (multidrug resistance proteins) and G (pleiotropic drug resistance transporters), whereas an increase in subgroup C (multidrug resistance-associated proteins) is evident in Tfichoderma virens. In contrast with mycoparasitic Tfichoderma species, C. rosea contains very few chitinases. Expression of six group B and group G ABC transporter genes was induced in C. rosea during exposure to the Fusafium mycotoxin zearalenone, the fungicide Boscalid or metabolites from the biocontrol bacterium Pseudomonas chiororaphis. The data suggest that tolerance toward secondary metabolites is a prominent feature in the biology of C. rosea."],["dc.identifier.doi","10.1093/gbe/evu292"],["dc.identifier.isi","000351607800005"],["dc.identifier.pmid","25575496"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/37980"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Oxford Univ Press"],["dc.relation.issn","1759-6653"],["dc.title","Insights on the Evolution of Mycoparasitism from the Genome of Clonostachys rosea"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS