Popova, Blagovesta

[["dc.bibliographiccitation.firstpage","14"],["dc.bibliographiccitation.journal","Environmental and Experimental Botany"],["dc.bibliographiccitation.lastpage","22"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Hoppenau, Clara E."],["dc.contributor.author","Tran, Van-Tuan"],["dc.contributor.author","Kusch, Harald"],["dc.contributor.author","Aßhauer, Kathrin P."],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-04-24T15:04:17Z"],["dc.date.available","2018-04-24T15:04:17Z"],["dc.date.issued","2014"],["dc.description.abstract","The vascular plant pathogen Verticillium dahliae colonizes the xylem fluid where only low nutrient concentrations are provided. Biosynthesis of the vitamin thiamine is connected to oxidative stress. The highly conserved VdThi4 protein is localized in fungal mitochondria and is required under vitamin B1 limiting conditions. Deletion of the corresponding VdTHI4 gene by Agrobacterium-mediated transformation resulted in strains which were impaired in growth on thiamine-free medium and could be rescued by additional vitamin supply or by complementation with the original gene after protoplastation. Furthermore, we show that VdThi4 increases fungal stress tolerance such as UV-damage or oxidative stress. The orthologous sti35 gene of Fusarium oxysporum, another vascular wilt fungus, was shown to be involved in stress response, however to be dispensable for pathogenicity on tomato. In contrast, VdTHI4 is required for fungal-induced tomato disease demonstrated by infection assays with a V. dahliae ΔVdTHI4 deletion strain which is still able to invade plants through the roots but is asymptomatic. Our results suggest remarkable differences between two vascular tomato pathogens where VdThi4 is required for pathogenicity of V. dahliae, whereas F. oxysporum still causes disease when the corresponding Sti35 protein is absent."],["dc.description.sponsorship","Federal Ministry of Education and Research (BMBF)"],["dc.description.sponsorship","Cluster of Excellence and DFG Research Center Nanoscale Microscopy and Molecular Physiology of the Brain"],["dc.identifier.doi","10.1016/j.envexpbot.2013.12.015"],["dc.identifier.other","http://www.sciencedirect.com/science/article/pii/S0098847213002268"],["dc.identifier.pii","S0098847213002268"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13764"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-575"],["dc.notes.status","zu prüfen"],["dc.relation.issn","0098-8472"],["dc.rights.uri","https://www.elsevier.com/tdm/userlicense/1.0/"],["dc.title","Verticillium dahliae VdTHI4, involved in thiazole biosynthesis, stress response and DNA repair functions, is required for vascular disease induction in tomato"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Magalhães, Rayne S S"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard H"],["dc.contributor.author","Outeiro, Tiago F"],["dc.contributor.author","Eleutherio, Elis C A"],["dc.date.accessioned","2020-12-10T18:19:12Z"],["dc.date.available","2020-12-10T18:19:12Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1093/femsyr/foy066"],["dc.identifier.eissn","1567-1364"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/75156"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","The trehalose protective mechanism during thermal stress in Saccharomyces cerevisiae: the roles of Ath1 and Agt1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","27567"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","The Journal of Biological Chemistry"],["dc.bibliographiccitation.lastpage","27579"],["dc.bibliographiccitation.volume","287"],["dc.contributor.author","Petroi, Doris"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Taheri-Talesh, Naimeh"],["dc.contributor.author","Irniger, Stefan"],["dc.contributor.author","Shahpasandzadeh, Hedieh"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Outeiro, Tiago F."],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T08:45:30Z"],["dc.date.available","2018-09-28T08:45:30Z"],["dc.date.issued","2012"],["dc.description.abstract","Parkinson disease is the second most common neurodegenerative disease. The molecular hallmark is the accumulation of proteinaceous inclusions termed Lewy bodies containing misfolded and aggregated α-synuclein. The molecular mechanism of clearance of α-synuclein aggregates was addressed using the bakers' yeast Saccharomyces cerevisiae as the model. Overexpression of wild type α-synuclein or the genetic variant A53T integrated into one genomic locus resulted in a gene copy-dependent manner in cytoplasmic proteinaceous inclusions reminiscent of the pathogenesis of the disease. In contrast, overexpression of the genetic variant A30P resulted only in transient aggregation, whereas the designer mutant A30P/A36P/A76P neither caused aggregation nor impaired yeast growth. The α-synuclein accumulation can be cleared after promoter shut-off by a combination of autophagy and vacuolar protein degradation. Whereas the proteasomal inhibitor MG-132 did not significantly inhibit aggregate clearance, treatment with phenylmethylsulfonyl fluoride, an inhibitor of vacuolar proteases, resulted in significant reduction in clearance. Consistently, a cim3-1 yeast mutant restricted in the 19 S proteasome regulatory subunit was unaffected in clearance, whereas an Δatg1 yeast mutant deficient in autophagy showed a delayed aggregate clearance response. A cim3-1Δatg1 double mutant was still able to clear aggregates, suggesting additional cellular mechanisms for α-synuclein clearance. Our data provide insight into the mechanisms yeast cells use for clearing different species of α-synuclein and demonstrate a higher contribution of the autophagy/vacuole than the proteasome system. This contributes to the understanding of how cells can cope with toxic and/or aggregated proteins and may ultimately enable the development of novel strategies for therapeutic intervention."],["dc.identifier.doi","10.1074/jbc.M112.361865"],["dc.identifier.pmid","22722939"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15838"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1083-351X"],["dc.title","Aggregate clearance of α-synuclein in Saccharomyces cerevisiae depends more on autophagosome and vacuole function than on the proteasome"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","168"],["dc.bibliographiccitation.journal","Diamond and Related Materials"],["dc.bibliographiccitation.lastpage","178"],["dc.bibliographiccitation.volume","93"],["dc.contributor.author","Merker, Daniel"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Bergfeldt, Thomas"],["dc.contributor.author","Weingärtner, Tobias"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Reithmaier, Johann Peter"],["dc.contributor.author","Popov, Cyril"],["dc.date.accessioned","2020-12-10T14:23:27Z"],["dc.date.available","2020-12-10T14:23:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1016/j.diamond.2019.02.003"],["dc.identifier.issn","0925-9635"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/71929"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","Antimicrobial propensity of ultrananocrystalline diamond films with embedded silver nanodroplets"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Simm, Dominic"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Waack, Stephan"],["dc.contributor.author","Kollmar, Martin"],["dc.date.accessioned","2022-07-01T07:34:51Z"],["dc.date.available","2022-07-01T07:34:51Z"],["dc.date.issued","2022"],["dc.description.abstract","Abstract Heterologous protein expression is an important method for analysing cellular functions of proteins, in genetic circuit engineering and in overexpressing proteins for biopharmaceutical applications and structural biology research. The degeneracy of the genetic code, which enables a single protein to be encoded by a multitude of synonymous gene sequences, plays an important role in regulating protein expression, but substantial uncertainty exists concerning the details of this phenomenon. Here we analyse the influence of a profiled codon usage adaptation approach on protein expression levels in the eukaryotic model organism Saccharomyces cerevisiae . We selected green fluorescent protein (GFP) and human α-synuclein (αSyn) as representatives for stable and intrinsically disordered proteins and representing a benchmark and a challenging test case. A new approach was implemented to design typical genes resembling the codon usage of any subset of endogenous genes. Using this approach, synthetic genes for GFP and αSyn were generated, heterologously expressed and evaluated in yeast. We demonstrate that GFP is expressed at high levels, and that the toxic αSyn can be adapted to endogenous, low-level expression. The new software is publicly available as a web-application for performing host-specific protein adaptations to a set of the most commonly used model organisms ( https://odysseus.motorprotein.de )."],["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.description.sponsorship","Open-Access-Publikationsfonds 2022"],["dc.identifier.doi","10.1038/s41598-022-13089-1"],["dc.identifier.pii","13089"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112027"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-581"],["dc.relation.eissn","2045-2322"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Design of typical genes for heterologous gene expression"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","S0022283621003910"],["dc.bibliographiccitation.firstpage","167162"],["dc.bibliographiccitation.issue","19"],["dc.bibliographiccitation.journal","Journal of Molecular Biology"],["dc.bibliographiccitation.volume","433"],["dc.contributor.author","Sirati, Nafiseh"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Molenaar, Martijn R."],["dc.contributor.author","Verhoek, Iris C."],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Kaloyanova, Dora V."],["dc.contributor.author","Helms, J. Bernd"],["dc.date.accessioned","2021-10-01T09:57:36Z"],["dc.date.available","2021-10-01T09:57:36Z"],["dc.date.issued","2021"],["dc.identifier.doi","10.1016/j.jmb.2021.167162"],["dc.identifier.pii","S0022283621003910"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89876"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-469"],["dc.relation.issn","0022-2836"],["dc.title","Dynamic and Reversible Aggregation of the Human CAP Superfamily Member GAPR-1 in Protein Inclusions in Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Juckert, Alexandra"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Braus, Gerhard"],["dc.date.accessioned","2018-11-07T09:20:13Z"],["dc.date.available","2018-11-07T09:20:13Z"],["dc.date.issued","2013"],["dc.format.extent","199"],["dc.identifier.isi","000327927400427"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28834"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th International Conference on Yeast Genetics and Molecular Biology"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","Nitration of tyrosine residues of alpha-synuclein increases aggregation and toxicity in yeast model of Parkinson disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Yeast"],["dc.bibliographiccitation.volume","30"],["dc.contributor.author","Shahpasandzadeh, Hedieh"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard"],["dc.date.accessioned","2018-11-07T09:20:12Z"],["dc.date.available","2018-11-07T09:20:12Z"],["dc.date.issued","2013"],["dc.format.extent","80"],["dc.identifier.isi","000327927400109"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/28827"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.publisher.place","Hoboken"],["dc.relation.conference","26th International Conference on Yeast Genetics and Molecular Biology"],["dc.relation.eventlocation","Frankfurt Main, GERMANY"],["dc.relation.issn","1097-0061"],["dc.relation.issn","0749-503X"],["dc.title","Interplay of post-translational modifications of alpha-synuclein in yeast model of Parkinson disease"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1142"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Eukaryotic Cell"],["dc.bibliographiccitation.lastpage","1154"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Herzog, Britta"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Jakobshagen, Antonia"],["dc.contributor.author","Shahpasandzadeh, Hedieh"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T08:38:51Z"],["dc.date.available","2018-09-28T08:38:51Z"],["dc.date.issued","2013"],["dc.description.abstract","Hac1 is the activator of the cellular response to the accumulation of unfolded proteins in the endoplasmic reticulum. Hac1 function requires the activity of Gcn4, which mainly acts as a regulator of the general amino acid control network providing Saccharomyces cerevisiae cells with amino acids. Here, we demonstrate novel functions of Hac1 and describe a mutual connection between Hac1 and Gcn4. Hac1 is required for induction of Gcn4-responsive promoter elements in haploid as well as diploid cells and therefore participates in the cellular amino acid supply. Furthermore, Hac1 and Gcn4 mutually influence their mRNA expression levels. Hac1 is also involved in FLO11 expression and adhesion upon amino acid starvation. Hac1 and Gcn4 act through the same promoter regions of the FLO11 flocculin. The results indicate an indirect effect of both transcription factors on FLO11 expression. Our data suggest a complex mutual cross talk between the Hac1- and Gcn4-controlled networks."],["dc.identifier.doi","10.1128/EC.00123-13"],["dc.identifier.pmid","23794510"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15837"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.eissn","1535-9786"],["dc.title","Mutual cross talk between the regulators Hac1 of the unfolded protein response and Gcn4 of the general amino acid control of Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","145"],["dc.bibliographiccitation.lastpage","156"],["dc.bibliographiccitation.seriesnr","1948"],["dc.contributor.author","Brás, Inês Caldeira"],["dc.contributor.author","Popova, Blagovesta"],["dc.contributor.author","Braus, Gerhard H."],["dc.contributor.author","Outeiro, Tiago Fleming"],["dc.contributor.editor","Bartels, Tim"],["dc.date.accessioned","2021-06-02T10:44:27Z"],["dc.date.available","2021-06-02T10:44:27Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/978-1-4939-9124-2_12"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87042"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-9124-2"],["dc.relation.isbn","978-1-4939-9123-5"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","Alpha-Synuclein : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1948"],["dc.title","Yeast-Based Screens to Target Alpha-Synuclein Toxicity"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]