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Kaever, Alexander
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Kaever, Alexander
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Kaever, Alexander
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Kaever, A.
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2014Journal Article [["dc.bibliographiccitation.firstpage","823"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","837"],["dc.bibliographiccitation.volume","202"],["dc.contributor.author","König, Stefanie"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Thurow, Corinna"],["dc.contributor.author","Karlovsky, Petr"],["dc.contributor.author","Gatz, Christiane"],["dc.contributor.author","Polle, Andrea"],["dc.contributor.author","Feußner, Ivo"],["dc.date.accessioned","2017-09-07T11:50:45Z"],["dc.date.available","2017-09-07T11:50:45Z"],["dc.date.issued","2014"],["dc.description.abstract","Summary - Verticillium longisporum is a soil‐borne vascular pathogen causing economic loss in rape. Using the model plant Arabidopsis this study analyzed metabolic changes upon fungal infection in order to identify possible defense strategies of Brassicaceae against this fungus. - Metabolite fingerprinting identified infection‐induced metabolites derived from the phenylpropanoid pathway. Targeted analysis confirmed the accumulation of sinapoyl glucosides, coniferin, syringin and lignans in leaves from early stages of infection on. At later stages, the amounts of amino acids increased. - To test the contribution of the phenylpropanoid pathway, mutants in the pathway were analyzed. The sinapate‐deficient mutant fah1‐2 showed stronger infection symptoms than wild‐type plants, which is most likely due to the lack of sinapoyl esters. Moreover, the coniferin accumulating transgenic plant UGT72E2‐OE was less susceptible. Consistently, sinapoyl glucose, coniferyl alcohol and coniferin inhibited fungal growth and melanization in vitro, whereas sinapyl alcohol and syringin did not. The amount of lignin was not significantly altered supporting the notion that soluble derivatives of the phenylpropanoid pathway contribute to defense. - These data show that soluble phenylpropanoids are important for the defense response of Arabidopsis against V. longisporum and that metabolite fingerprinting is a valuable tool to identify infection‐relevant metabolic markers."],["dc.identifier.doi","10.1111/nph.12709"],["dc.identifier.gro","3147731"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5128"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.notes.submitter","chake"],["dc.relation.issn","0028-646X"],["dc.title","Soluble phenylpropanoids are involved in the defense response of Arabidopsis against Verticillium longisporum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]Details DOI2012Journal Article [["dc.bibliographiccitation.firstpage","1086"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","1097"],["dc.bibliographiccitation.volume","196"],["dc.contributor.author","Koenig, Stefanie"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Schwarz, Marnie"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Iven, Tim"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Ternes, Philipp"],["dc.contributor.author","Karlovsky, Petr"],["dc.contributor.author","Lipka, Volker"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T09:03:07Z"],["dc.date.available","2018-11-07T09:03:07Z"],["dc.date.issued","2012"],["dc.description.abstract","In Arabidopsis, the fatty acid moiety of sphingolipids is mainly alpha-hydroxylated. The consequences of a reduction in this modification were analysed. Mutants of both Fatty Acid Hydroxylase genes (AtFAH1 and AtFAH2) were analysed for sphingolipid profiles. To elucidate further consequences of the mutations, metabolic analyses were performed and the influence on pathogen defence was determined. Ceramide and glucosylceramide profiles of double-mutant plants showed a reduction in sphingolipids with alpha-hydroxylated fatty acid moieties, and an accumulation of sphingolipids without these moieties. In addition, the free trihydroxylated long-chain bases and ceramides were increased by five- and ten-fold, respectively, whereas the amount of glucosylceramides was decreased by 25%. Metabolite analysis of the double mutant revealed salicylates as enriched metabolites. Infection experiments supported the metabolic changes, as the double mutant showed an enhanced disease-resistant phenotype for infection with the obligate biotrophic pathogen Golovinomyces cichoracearum. In summary, these results suggest that fatty acid hydroxylation of ceramides is important for the biosynthesis of complex sphingolipids. Its absence leads to the accumulation of long-chain bases and ceramides as their precursors. This increases salicylate levels and resistance towards obligate biotrophic fungal pathogens, confirming a role of sphingolipids in salicylic acid-dependent defence reactions."],["dc.description.sponsorship","DFG Research Unit FOR546 [Fe 446/6, Ka 1209/3, FL3 INST 186/822-1]"],["dc.identifier.doi","10.1111/j.1469-8137.2012.04351.x"],["dc.identifier.isi","000310676400016"],["dc.identifier.pmid","23025549"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/24836"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","0028-646X"],["dc.title","Arabidopsis mutants of sphingolipid fatty acid alpha-hydroxylases accumulate ceramides and salicylates"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2014Journal Article [["dc.bibliographiccitation.firstpage","406"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","420"],["dc.bibliographiccitation.volume","29"],["dc.contributor.author","Sarikaya-Bayram, Oezlem"],["dc.contributor.author","Bayram, Oezguer"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Kim, Jong-Hwa"],["dc.contributor.author","Kim, Hee-Seo"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Chae, Keon-Sang"],["dc.contributor.author","Han, Dong-Min"],["dc.contributor.author","Han, Kap-Hoon"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:39:57Z"],["dc.date.available","2018-11-07T09:39:57Z"],["dc.date.issued","2014"],["dc.description.abstract","Epigenetic and transcriptional control of gene expression must be coordinated in response to external signals to promote alternative multicellular developmental programs. The membrane-associated trimeric complex VapA-VipC-VapB controls a signal transduction pathway for fungal differentiation. The VipC-VapB methyltransferases are tethered to the membrane by the FYVE-like zinc finger protein VapA, allowing the nuclear VelB-VeA-LaeA complex to activate transcription for sexual development. Once the release from VapA is triggered, VipC-VapB is transported into the nucleus. VipC-VapB physically interacts with VeA and reduces its nuclear import and protein stability, thereby reducing the nuclear VelB-VeA-LaeA complex. Nuclear VapB methyltransferase diminishes the establishment of facultative heterochromatin by decreasing histone 3 lysine 9 trimethylation (H3K9me3). This favors activation of the regulatory genes brlA and abaA, which promote the asexual program. The VapA-VipC-VapB methyltransferase pathway combines control of nuclear import and stability of transcription factors with histone modification to foster appropriate differentiation responses."],["dc.identifier.doi","10.1016/j.devcel.2014.03.020"],["dc.identifier.isi","000336608600005"],["dc.identifier.pmid","24871947"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33407"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1878-1551"],["dc.relation.issn","1534-5807"],["dc.title","Membrane-Bound Methyltransferase Complex VapA-VipC-VapB Guides Epigenetic Control of Fungal Development"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2014Journal Article [["dc.bibliographiccitation.firstpage","227"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The Plant Journal"],["dc.bibliographiccitation.lastpage","240"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Gamir, Jordi"],["dc.contributor.author","Pastor, Victoria"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Cerezo, Miguel"],["dc.contributor.author","Flors, Victor"],["dc.date.accessioned","2018-11-07T09:41:59Z"],["dc.date.available","2018-11-07T09:41:59Z"],["dc.date.issued","2014"],["dc.description.abstract","Priming is a physiological state for protection of plants against a broad range of pathogens, and is achieved through stimulation of the plant immune system. Various stimuli, such as beneficial microbes and chemical induction, activate defense priming. In the present study, we demonstrate that impairment of the high-affinity nitrate transporter 2.1 (encoded by NRT2.1) enables Arabidopsis to respond more quickly and strongly to Plectosphaerella cucumerina attack, leading to enhanced resistance. The Arabidopsis thaliana mutant lin1 (affected in NRT2.1) is a priming mutant that displays constitutive resistance to this necrotroph, with no associated developmental or growth costs. Chemically induced priming by beta-aminobutyric acid treatment, the constitutive priming mutant ocp3 and the constitutive priming present in the lin1 mutant result in a common metabolic profile within the same plant-pathogen interactions. The defense priming significantly affects sugar metabolism, cell-wall remodeling and shikimic acid derivatives levels, and results in specific changes in the amino acid profile and three specific branches of Trp metabolism, particularly accumulation of indole acetic acid, indole-3-carboxaldehyde and camalexin, but not the indolic glucosinolates. Metabolomic analysis facilitated identification of three metabolites in the priming fingerprint: galacturonic acid, indole-3-carboxylic acid and hypoxanthine. Treatment of plants with the latter two metabolites by soil drenching induced resistance against P.cucumerina, demonstrating that these compounds are key components of defense priming against this necrotrophic fungus. Here we demonstrate that indole-3-carboxylic acid induces resistance by promoting papillae deposition and H2O2 production, and that this is independent of PR1, VSP2 and PDF1.2 priming."],["dc.identifier.doi","10.1111/tpj.12465"],["dc.identifier.isi","000333922300005"],["dc.identifier.pmid","24506441"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33852"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1365-313X"],["dc.relation.issn","0960-7412"],["dc.title","Targeting novel chemical and constitutive primed metabolites against Plectosphaerella cucumerina"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2014Journal Article [["dc.bibliographiccitation.firstpage","565"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","New Phytologist"],["dc.bibliographiccitation.lastpage","581"],["dc.bibliographiccitation.volume","202"],["dc.contributor.author","Van-Tuan Tran, Van-Tuan Tran"],["dc.contributor.author","Braus-Stromeyer, Susanna A."],["dc.contributor.author","Kusch, Harald"],["dc.contributor.author","Reusche, Michael"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Kuehn, Anika"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Landesfeind, Manuel"],["dc.contributor.author","Asshauer, Kathrin"],["dc.contributor.author","Tech, Maike"],["dc.contributor.author","Hoff, Katharina J."],["dc.contributor.author","Pena-Centeno, Tonatiuh"],["dc.contributor.author","Stanke, Mario"],["dc.contributor.author","Lipka, Volker"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-11-07T09:41:36Z"],["dc.date.available","2018-11-07T09:41:36Z"],["dc.date.issued","2014"],["dc.description.abstract"," Six transcription regulatory genes of the Verticillium plant pathogen, which reprogrammed nonadherent budding yeasts for adhesion, were isolated by a genetic screen to identify control elements for early plant infection.Verticillium transcription activator of adhesion Vta2 is highly conserved in filamentous fungi but not present in yeasts. The Magnaporthe grisea ortholog conidiation regulator Con7 controls the formation of appressoria which are absent in Verticillium species. Vta2 was analyzed by using genetics, cell biology, transcriptomics, secretome proteomics and plant pathogenicity assays. Nuclear Vta2 activates the expression of the adhesin-encoding yeast flocculin genes FLO1 and FLO11. Vta2 is required for fungal growth of Verticillium where it is a positive regulator of conidiation. Vta2 is mandatory for accurate timing and suppression of microsclerotia as resting structures. Vta2 controls expression of 270 transcripts, including 10 putative genes for adhesins and 57 for secreted proteins. Vta2 controls the level of 125 secreted proteins, including putative adhesins or effector molecules and a secreted catalase-peroxidase. Vta2 is a major regulator of fungal pathogenesis, and controls host-plant root infection and H2O2 detoxification.Verticillium impaired in Vta2 is unable to colonize plants and induce disease symptoms. Vta2 represents an interesting target for controlling the growth and development of these vascular pathogens."],["dc.identifier.doi","10.1111/nph.12671"],["dc.identifier.isi","000333060500027"],["dc.identifier.pmid","24433459"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/33771"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1469-8137"],["dc.relation.issn","0028-646X"],["dc.title","Verticillium transcription activator of adhesion Vta2 suppresses microsclerotia formation and is required for systemic infection of plant roots"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2009Conference Abstract [["dc.bibliographiccitation.journal","Chemistry and Physics of Lipids"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Goebel, C."],["dc.contributor.author","Feussner, Kristin"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Morgenstern, Burkhard"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2018-11-07T11:25:53Z"],["dc.date.available","2018-11-07T11:25:53Z"],["dc.date.issued","2009"],["dc.format.extent","S26"],["dc.identifier.doi","10.1016/j.chemphyslip.2009.06.024"],["dc.identifier.isi","000269390600071"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56729"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Ireland Ltd"],["dc.publisher.place","Clare"],["dc.relation.conference","50th International Conference on Bioscience of Lipids"],["dc.relation.eventlocation","Regenburg, GERMANY"],["dc.relation.issn","0009-3084"],["dc.title","Identification of metabolic changes after wounding in Arabidopsis thaliana by an unbiased UPLC-MS approach"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI WOS2016Journal Article [["dc.bibliographiccitation.firstpage","68"],["dc.bibliographiccitation.journal","Life Sciences"],["dc.bibliographiccitation.lastpage","73"],["dc.bibliographiccitation.volume","156"],["dc.contributor.author","Tschirner, Sarah K."],["dc.contributor.author","Baehre, Heike"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Schneider, Erich H."],["dc.contributor.author","Seifert, Roland"],["dc.contributor.author","Kaever, Volkhard"],["dc.date.accessioned","2018-11-07T10:12:31Z"],["dc.date.available","2018-11-07T10:12:31Z"],["dc.date.issued","2016"],["dc.description.abstract","Aims: Lesch-Nyhan disease (LND) is characterized by hyperuricemia as well as neurological and neuropsychiatric symptoms including repetitive self-injurious behavior. Symptoms are caused by a deficiency of the enzyme hypoxanthine-guanine phosphoribosyltransferase (HPRT) as a result of a mutation on the X chromosome. To elucidate the pathophysiology of LND, we performed a metabolite screening for brain and serum extracts from HPRT knockout mice as an animal model for LND. Main methods: Analyses were performed by high performance liquid chromatography (HPLC)-coupled quadrupole time-of-flight mass spectrometry (QTOF-MS). Key findings: In brain extracts, we found six metabolites with significantly different contents in wild-type and HPRT-deficient mice. Two compounds we could identify as 5-aminoimidazole-4-carboxamide ribotide (AICAR) and 1-methylimidazole-4-acetic acid (1-MI4AA). Whereas AICAR was accumulated in brains of HPRT knockout mice, 1-MI4AA was decreased in these mice. Significance: Both metabolites play a role in histidine metabolism and, as a consequence, histamine metabolism. AICAR, in addition, is part of the purine metabolism. Our findings may help to better understand the mechanisms leading to the behavioral phenotype of LND. (C) 2016 Elsevier Inc. All rights reserved."],["dc.identifier.doi","10.1016/j.lfs.2016.05.031"],["dc.identifier.isi","000377540900009"],["dc.identifier.pmid","27221022"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/40250"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Pergamon-elsevier Science Ltd"],["dc.relation.issn","1879-0631"],["dc.relation.issn","0024-3205"],["dc.title","Non-targeted metabolomics by high resolution mass spectrometry in HPRT knockout mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details DOI PMID PMC WOS2010Journal Article [["dc.bibliographiccitation.firstpage","964"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Molecular Microbiology"],["dc.bibliographiccitation.lastpage","979"],["dc.bibliographiccitation.volume","78"],["dc.contributor.author","Nahlik, Krystyna"],["dc.contributor.author","Dumkow, Marc"],["dc.contributor.author","Bayram, Ozgür"],["dc.contributor.author","Helmstaedt, Kerstin"],["dc.contributor.author","Busch, Silke"],["dc.contributor.author","Valerius, Oliver"],["dc.contributor.author","Gerke, Jennifer"],["dc.contributor.author","Hoppert, Michael"],["dc.contributor.author","Schwier, Elke U."],["dc.contributor.author","Opitz, Lennart"],["dc.contributor.author","Westermann, Mieke"],["dc.contributor.author","Grond, Stephanie"],["dc.contributor.author","Feussner, Kirstin"],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Meinicke, Peter"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Braus, Gerhard H."],["dc.date.accessioned","2018-09-28T09:12:22Z"],["dc.date.available","2018-09-28T09:12:22Z"],["dc.date.issued","2010"],["dc.description.abstract","The COP9 signalosome complex (CSN) is a crucial regulator of ubiquitin ligases. Defects in CSN result in embryonic impairment and death in higher eukaryotes, whereas the filamentous fungus Aspergillus nidulans survives without CSN, but is unable to complete sexual development. We investigated overall impact of CSN activity on A. nidulans cells by combined transcriptome, proteome and metabolome analysis. Absence of csn5/csnE affects transcription of at least 15% of genes during development, including numerous oxidoreductases. csnE deletion leads to changes in the fungal proteome indicating impaired redox regulation and hypersensitivity to oxidative stress. CSN promotes the formation of asexual spores by regulating developmental hormones produced by PpoA and PpoC dioxygenases. We identify more than 100 metabolites, including orsellinic acid derivatives, accumulating preferentially in the csnE mutant. We also show that CSN is required to activate glucanases and other cell wall recycling enzymes during development. These findings suggest a dual role for CSN during development: it is required early for protection against oxidative stress and hormone regulation and is later essential for control of the secondary metabolism and cell wall rearrangement."],["dc.identifier.doi","10.1111/j.1365-2958.2010.07384.x"],["dc.identifier.pmid","21062371"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/15841"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.relation.eissn","1365-2958"],["dc.title","The COP9 signalosome mediates transcriptional and metabolic response to hormones, oxidative stress protection and cell wall rearrangement during fungal development"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]Details DOI PMID PMC2013Conference Abstract [["dc.bibliographiccitation.journal","Naunyn-Schmiedeberg s Archives of Pharmacology"],["dc.bibliographiccitation.volume","386"],["dc.contributor.author","Burhenne, H."],["dc.contributor.author","Tschirner, Sarah K."],["dc.contributor.author","Kuhn, M."],["dc.contributor.author","Kaever, Alexander"],["dc.contributor.author","Seifert, R."],["dc.contributor.author","Kaever, Volkhard"],["dc.date.accessioned","2018-11-07T09:28:53Z"],["dc.date.available","2018-11-07T09:28:53Z"],["dc.date.issued","2013"],["dc.format.extent","S14"],["dc.identifier.isi","000209476400052"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30893"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Springer"],["dc.publisher.place","New york"],["dc.relation.issn","1432-1912"],["dc.relation.issn","0028-1298"],["dc.title","Metabolic alterations in Lesch-Nyhan syndrome"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]Details WOS