Pöggeler, Stefanie

[["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"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","830"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","834"],["dc.bibliographiccitation.volume","355"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T11:03:12Z"],["dc.date.available","2018-11-07T11:03:12Z"],["dc.date.issued","2007"],["dc.description.abstract","Inteins are internal protein domains found inside the coding region of different proteins. They can autocatalytically self-excise from their host protein and ligate the protein flanks, called exteins, with a peptide bond via a post-translational process called protein cis-splicing. In contrast, protein trans-splicing involves inteins split into an N- and a C-terminal domain. Both domains are synthesized as two separate components and each joined to an extein; the intein domains can reassemble and link the joined exteins into one functional protein. In this study, we introduced three split sites into the PRP8 mini-intein of Penicillium chrysogenum and demonstrated for the first time trans-splicing of a fungal PRPS intein. Two of the sites introduced allowed splicing to occur in trans while the third was not functional. (c) 2007 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.bbrc.2007.02.035"],["dc.identifier.isi","000245001300038"],["dc.identifier.pmid","17316565"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51561"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","0006-291X"],["dc.title","Trans-splicing of an artificially split fungal mini-intein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","239"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Biochemical and Biophysical Research Communications"],["dc.bibliographiccitation.lastpage","243"],["dc.bibliographiccitation.volume","366"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Doering, Kristin"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T11:18:27Z"],["dc.date.available","2018-11-07T11:18:27Z"],["dc.date.issued","2008"],["dc.description.abstract","Inteins are internal protein splicing elements that can autocatalytically self-excise from their host protein and ligate the protein flanks (exteins) with a peptide bond. Large inteins comprise independent protein splicing and endonuclease domains whereas mini-inteins lack the central endonuclease domain. To identify mini-intein domains that are essential for protein splicing, deletions were introduced at different sites of the 157-aa PRPS mini-intein of Penicillium chrysogenum. The removal of eight and six amino acids at two different sites resulted in a functional eukaryotic mini-intein of only 143 aa. (c) 2007 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.bbrc.2007.11.126"],["dc.identifier.isi","000252392400038"],["dc.identifier.pmid","18054328"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55036"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Inc Elsevier Science"],["dc.relation.issn","0006-291X"],["dc.title","Minimization of a eukaryotic mini-intein"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","52"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Basic Microbiology"],["dc.bibliographiccitation.lastpage","57"],["dc.bibliographiccitation.volume","49"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Pelikan, Constantin"],["dc.contributor.author","Nolting, Nicole"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T08:33:07Z"],["dc.date.available","2018-11-07T08:33:07Z"],["dc.date.issued","2009"],["dc.description.abstract","Inteins are protein-intervening sequences that are translated with the host protein and can self-excise themselves post-translationally in an autocatalytic process. The flanking regions called exteins - are then re-ligated with a new peptide bond, resulting in a mature host protein. Previously, we have identified inteins in the highly conserved 3.2 region of the PRP8 protein from species of the genus Penicillium. These inteins are integrated at the same position as that which has recently been described in PRP8 proteins from different strains of Cryptococcus neoformans and several ascomycetes. In this study, we investigated the presence of PRP8 inteins in four members of the genus Eupenicillium. Two species of this genus, Eupenicillium crustaceum and Eupenicillium baarnense, contain an intein at the same insertion site. Both inteins are mini-inteins and undergo self-splicing when heterologously expressed with a model host protein in Escherichia coli. Interestingly, we identified introns in the prp8-sequence encoding the 3.2 regions of the PRP8 protein in Eupenicillium meridianum and Eupenicillium terrenum. The introns are located 13 bps and 15 bps downstream of the putative intein insertion site. Here, we consider that the lack of inteins in these two species might be due to the prevention of endonuclease-mediated intein propagation in the intron-containing prp8-sequences."],["dc.identifier.doi","10.1002/jobm.200800168"],["dc.identifier.isi","000264348600006"],["dc.identifier.pmid","19253333"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17501"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-v C H Verlag Gmbh"],["dc.relation.issn","0233-111X"],["dc.title","Inteins and introns within the prp8-gene of four Eupenicillium species"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","479"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Applied Microbiology and Biotechnology"],["dc.bibliographiccitation.lastpage","489"],["dc.bibliographiccitation.volume","87"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T08:42:25Z"],["dc.date.available","2018-11-07T08:42:25Z"],["dc.date.issued","2010"],["dc.description.abstract","Inteins are internal protein elements that self-excise from their host protein and catalyze ligation of the flanking sequences (exteins) with a peptide bond. They are found in organisms in all three domains of life, and in viral proteins. Intein excision is a posttranslational process that does not require auxiliary enzymes or cofactors. This self-excision process is called protein splicing, by analogy to the splicing of RNA introns from pre-mRNA. Protein splicing involves only four intramolecular reactions, and a small number of key catalytic residues in the intein and exteins. Protein-splicing can also occur in trans. In this case, the intein is separated into N- and C-terminal domains, which are synthesized as separate components, each joined to an extein. The intein domains reassemble and link the joined exteins into a single functional protein. Understanding the cis- and trans-protein splicing mechanisms led to the development of intein-mediated protein-engineering applications, such as protein purification, ligation, cyclization, and selenoprotein production. This review summarizes the catalytic activities and structures of inteins, and focuses on the advantages of some recent intein applications in molecular biology and biotechnology."],["dc.identifier.doi","10.1007/s00253-010-2628-x"],["dc.identifier.isi","000277959500009"],["dc.identifier.pmid","20449740"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/4237"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19696"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0175-7598"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Inteins, valuable genetic elements in molecular biology and biotechnology"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","211"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Current Genetics"],["dc.bibliographiccitation.lastpage","222"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T08:30:59Z"],["dc.date.available","2018-11-07T08:30:59Z"],["dc.date.issued","2009"],["dc.description.abstract","The ubiquitous metalloenzyme carbonic anhydrase (CA) catalyzes the interconversion of carbon dioxide and bicarbonate. This enzyme has been investigated in mammals, plants, algae, bacteria, archaea and fungi. Based on distinct structural characteristics, CAs can be assigned to five independently evolved classes (alpha, beta, gamma, delta and zeta). beta-CAs can be further subdivided into plant-type and cab-type sub-classes. The recent characterization of CAs in fungi led us to initiate a systematic search for these enzymes in filamentous ascomycetes. The genomes of basidiomycetes and hemiascomycetous yeasts contain only beta-CAs, while the filamentous ascomycetes also possess genes encoding alpha-class CAs. Here, we present a phylogenetic analysis of 97 fungal CA sequences that addresses the diversification of fungal CAs. During evolution various gene duplication and gene loss events seem to be the cause for the multiplicity of CAs in filamentous ascomycetes. Our data revealed that during the evolution of filamentous ascomycetes, a gene encoding the plant-type beta-CA was duplicated, resulting in two closely related isoforms, one with and one without an N-terminal mitochondrial target sequence (MTS). The acquisition of the MTS most likely took place after the gene duplication event and after the evolutionary separation of the fungal orders Sordariales and Eurotiales."],["dc.identifier.doi","10.1007/s00294-009-0238-x"],["dc.identifier.isi","000265092000010"],["dc.identifier.pmid","19296112"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3498"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/17018"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.relation.issn","0172-8083"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Evolution of carbonic anhydrases in fungi"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1458"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Fungal Genetics and Biology"],["dc.bibliographiccitation.lastpage","1469"],["dc.bibliographiccitation.volume","45"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T11:09:27Z"],["dc.date.available","2018-11-07T11:09:27Z"],["dc.date.issued","2008"],["dc.description.abstract","Cyanase degrades toxic cyanate to NH3 and CO2 in a bicarbonate-dependent reaction. High concentrations of cyanate are fairly toxic to organisms. Here, we characterize a eukaryotic cyanase for the first time. We have isolated the cyn1 gene encoding a cyanase from the filamentous ascomycete Sordaria macrospora and functionally characterized the cyn1 product after heterologous expression in Escherichia coli. Site-directed mutagenesis confirmed a predicted catalytic centre of three conserved amino-acids. A Delta cyn1 knockout in S. macrospora was totally devoid of cyanase activity and showed an increased sensitivity to exogenously supplied cyanate in an arginine-depleted medium, defects in ascospore germination, but no other obvious morphological phenotype. By means of real-time PCR we have demonstrated that the transcriptional level of cyn1 is markedly elevated in the presence of cyanate and down-regulated by addition of arginine. The putative functions of cyanase in fungi are discussed. (c) 2008 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.fgb.2008.08.005"],["dc.identifier.isi","000261220400002"],["dc.identifier.pmid","18796334"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/53009"],["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","A cyanase is transcriptionally regulated by arginine and involved in cyanate decomposition in Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","873"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","European Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","887"],["dc.bibliographiccitation.volume","89"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Bernhards, Yasmine"],["dc.contributor.author","Schaefers, Christian"],["dc.contributor.author","Varghese, Jans Manjali"],["dc.contributor.author","Nolting, Nicole"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T08:36:09Z"],["dc.date.available","2018-11-07T08:36:09Z"],["dc.date.issued","2010"],["dc.description.abstract","In fungi, the homoeodomain protein STE12 controls diverse developmental processes, and derives its regulatory specificity from different protein interactions. We recently showed that in the homothallic ascomycete Sordaria macrospora, STE12 is essential for ascospore development, and is able to interact with the alpha-domain mating-type protein SMTA-1 and the MADS box protein MCM1. To further evaluate the functional roles of STE12, we used the yeast two-hybrid approach to identify new STE12-interacting partners. Using STE12 as bait, a small, serine-threonine-rich protein (designated STE12-interacting protein 2, SIP2) was identified. SIP2 is conserved among members of the fungal class Sordariomyceres. In vivo localization studies revealed that SIP2 was targeted to the nucleus and cytoplasm. The STE12/SIP2 interaction was further confirmed in vivo by bimolecular fluorescence complementation. Nuclear localization of SIP2 was apparently mediated by STE12. Unlike deletion of ste12, deletion of sip2 in S. macrospora led to only a slight decrease in ascospore germination, and no other obvious morphological phenotype. In comparison to the Delta stel2 single knockout strain, ascospore germination was significantly increased in a Delta sip2/ste12 double knockout strain. Our data provide evidence for a regulatory role of the novel fungal protein SIP2 in ascospore germination. (C) 2010 Elsevier GmbH. All rights reserved."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft (Bonn, Germany) [PO523/3-2]"],["dc.identifier.doi","10.1016/j.ejcb.2010.06.014"],["dc.identifier.isi","000286448000003"],["dc.identifier.pmid","20701996"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18243"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Gmbh, Urban & Fischer Verlag"],["dc.relation.issn","0171-9335"],["dc.title","The small serine-threonine protein SIP2 interacts with STE12 and is involved in ascospore germination in Sordaria macrospora"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","931"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","944"],["dc.bibliographiccitation.volume","92"],["dc.contributor.author","Lehneck, Ronny"],["dc.contributor.author","Elleuche, Skander"],["dc.contributor.author","Poeggeler, Stefanie"],["dc.date.accessioned","2018-11-07T09:39:27Z"],["dc.date.available","2018-11-07T09:39:27Z"],["dc.date.issued","2014"],["dc.description.abstract","The rapid interconversion of carbon dioxide and bicarbonate (hydrogen carbonate) is catalysed by metalloenzymes termed carbonic anhydrases (CAs). CAs have been identified in all three domains of life and can be divided into five evolutionarily unrelated classes (, , , and) that do not share significant sequence similarities. The function of the mammalian, prokaryotic and plant -CAs has been intensively studied but the function of CAs in filamentous ascomycetes is mostly unknown. The filamentous ascomycete Sordaria macrospora codes for four CAs, three of the -class and one of the -class. Here, we present a functional analysis of CAS4, the S. macrospora -class CA. The CAS4 protein was post-translationally glycosylated and secreted. The knockout strain cas4 had a significantly reduced rate of ascospore germination. To determine the cas genes required for S.macrospora growth under ambient air conditions, we constructed double and triple mutations of the four cas genes in all possible combinations and a quadruple mutant. Vegetative growth rate of the quadruple mutant lacking all cas genes was drastically reduced compared to the wild type and invaded the agar under normal air conditions. Likewise the fruiting bodies were embedded in the agar and completely devoid of mature ascospores."],["dc.identifier.doi","10.1111/mmi.12607"],["dc.identifier.isi","000337560500004"],["dc.identifier.pmid","24720701"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33285"],["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","The filamentous ascomycete Sordaria macrospora can survive in ambient air without carbonic anhydrases"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]