Pöggeler, Stefanie

[["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","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"]]