Feußner, Ivo

[["dc.bibliographiccitation.artnumber","e1007734"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","PLOS Pathogens"],["dc.bibliographiccitation.volume","15"],["dc.contributor.author","Pinter, Niko"],["dc.contributor.author","Hach, Christina Andrea"],["dc.contributor.author","Hampel, Martin"],["dc.contributor.author","Rekhter, Dmitrij"],["dc.contributor.author","Zienkiewicz, Krzysztof"],["dc.contributor.author","Feußner, Ivo"],["dc.contributor.author","Poehlein, Anja"],["dc.contributor.author","Daniel, Rolf"],["dc.contributor.author","Finkernagel, Florian"],["dc.contributor.author","Heimel, Kai"],["dc.date.accessioned","2019-07-09T11:51:17Z"],["dc.date.available","2019-07-09T11:51:17Z"],["dc.date.issued","2019"],["dc.description.abstract","The corn smut fungus Ustilago maydis requires the unfolded protein response (UPR) to maintain homeostasis of the endoplasmic reticulum (ER) during the biotrophic interaction with its host plant Zea mays (maize). Crosstalk between the UPR and pathways controlling pathogenic development is mediated by protein-protein interactions between the UPR regulator Cib1 and the developmental regulator Clp1. Cib1/Clp1 complex formation results in mutual modification of the connected regulatory networks thereby aligning fungal proliferation in planta, efficient effector secretion with increased ER stress tolerance and long-term UPR activation in planta. Here we address UPR-dependent gene expression and its modulation by Clp1 using combinatorial RNAseq/ChIPseq analyses. We show that increased ER stress resistance is connected to Clp1-dependent alterations of Cib1 phosphorylation, protein stability and UPR gene expression. Importantly, we identify by deletion screening of UPR core genes the signal peptide peptidase Spp1 as a novel key factor that is required for establishing a compatible biotrophic interaction between U. maydis and its host plant maize. Spp1 is dispensable for ER stress resistance and vegetative growth but requires catalytic activity to interfere with the plant defense, revealing a novel virulence specific function for signal peptide peptidases in a biotrophic fungal/plant interaction."],["dc.identifier.doi","10.1371/journal.ppat.1007734"],["dc.identifier.pmid","30998787"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16094"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59916"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","572"],["dc.title","Signal peptide peptidase activity connects the unfolded protein response to plant defense suppression by Ustilago maydis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","53"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.journal","Biotechnology for Biofuels"],["dc.bibliographiccitation.lastpage","14"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Yu, Dan"],["dc.contributor.author","Hornung, Ellen"],["dc.contributor.author","Iven, Tim"],["dc.contributor.author","Feussner, Ivo"],["dc.date.accessioned","2019-07-09T11:45:15Z"],["dc.date.available","2019-07-09T11:45:15Z"],["dc.date.issued","2018"],["dc.description.abstract","Background: Biotechnology enables the production of high-valued industrial feedstocks from plant seed oil. The plant-derived wax esters with long-chain monounsaturated acyl moieties, like oleyl oleate, have favorite properties for lubrication. For biosynthesis of wax esters using acyl-CoA substrates, expressions of a fatty acyl reductase (FAR) and a wax synthase (WS) in seeds are sufficient. Results: For optimization of the enzymatic activity and subcellular localization of wax ester synthesis enzymes, two fusion proteins were created, which showed wax ester-forming activities in Saccharomyces cerevisiae. To promote the formation of oleyl oleate in seed oil, WSs from Acinetobactor baylyi (AbWSD1) and Marinobacter aquaeolei (MaWS2), as well as the two created fusion proteins were tested in Arabidopsis to evaluate their abilities and substrate preference for wax ester production. The tested seven enzyme combinations resulted in different yields and compositions of wax esters. Expression of a FAR of Marinobacter aquaeolei (MaFAR) with AbWSD1 or MaWS2 led to a high incorporation of C18 substrates in wax esters. The MaFAR/TMMmAWAT2-AbWSD1 combination resulted in the incorporation of more C18:1 alcohol and C18:0 acyl moieties into wax esters compared with MaFAR/AbWSD1. The fusion protein of a WS from Simmondsia chinensis (ScWS) with MaFAR exhibited higher specificity toward C20:1 substrates in preference to C18:1 substrates. Expression of MaFAR/AbWSD1 in the Arabidopsis fad2 fae1 double mutant resulted in the accumulation of oleyl oleate (18:1/18:1) in up to 62 mol% of total wax esters in seed oil, which was much higher than the 15 mol% reached by MaFAR/AbWSD1 in Arabidopsis Col-0 background. In order to increase the level of oleyl oleate in seed oil of Camelina, lines expressing MaFAR/ScWS were crossed with a transgenic high oleate line. The resulting plants accumulated up to >40 mg g seed-1 of wax esters, containing 27-34 mol% oleyl oleate. Conclusions: The overall yields and the compositions of wax esters can be strongly affected by the availability of acyl-CoA substrates and to a lesser extent, by the characteristics of wax ester synthesis enzymes. For synthesis of oleyl oleate in plant seed oil, appropriate wax ester synthesis enzymes with high catalytic efficiency and desired substrate specificity should be expressed in plant cells; meanwhile, high levels of oleic acid-derived substrates need to be supplied to these enzymes by modifying the fatty acid profile of developing seeds."],["dc.description.abstract","Background: Biotechnology enables the production of high-valued industrial feedstocks from plant seed oil. The plant-derived wax esters with long-chain monounsaturated acyl moieties, like oleyl oleate, have favorite properties for lubrication. For biosynthesis of wax esters using acyl-CoA substrates, expressions of a fatty acyl reductase (FAR) and a wax synthase (WS) in seeds are sufficient. Results: For optimization of the enzymatic activity and subcellular localization of wax ester synthesis enzymes, two fusion proteins were created, which showed wax ester-forming activities in Saccharomyces cerevisiae. To promote the formation of oleyl oleate in seed oil, WSs from Acinetobactor baylyi (AbWSD1) and Marinobacter aquaeolei (MaWS2), as well as the two created fusion proteins were tested in Arabidopsis to evaluate their abilities and substrate preference for wax ester production. The tested seven enzyme combinations resulted in different yields and compositions of wax esters. Expression of a FAR of Marinobacter aquaeolei (MaFAR) with AbWSD1 or MaWS2 led to a high incorporation of C18 substrates in wax esters. The MaFAR/TMMmAWAT2-AbWSD1 combination resulted in the incorporation of more C18:1 alcohol and C18:0 acyl moieties into wax esters compared with MaFAR/AbWSD1. The fusion protein of a WS from Simmondsia chinensis (ScWS) with MaFAR exhibited higher specificity toward C20:1 substrates in preference to C18:1 substrates. Expression of MaFAR/AbWSD1 in the Arabidopsis fad2 fae1 double mutant resulted in the accumulation of oleyl oleate (18:1/18:1) in up to 62 mol% of total wax esters in seed oil, which was much higher than the 15 mol% reached by MaFAR/AbWSD1 in Arabidopsis Col-0 background. In order to increase the level of oleyl oleate in seed oil of Camelina, lines expressing MaFAR/ScWS were crossed with a transgenic high oleate line. The resulting plants accumulated up to >40 mg g seed-1 of wax esters, containing 27-34 mol% oleyl oleate. Conclusions: The overall yields and the compositions of wax esters can be strongly affected by the availability of acyl-CoA substrates and to a lesser extent, by the characteristics of wax ester synthesis enzymes. For synthesis of oleyl oleate in plant seed oil, appropriate wax ester synthesis enzymes with high catalytic efficiency and desired substrate specificity should be expressed in plant cells; meanwhile, high levels of oleic acid-derived substrates need to be supplied to these enzymes by modifying the fatty acid profile of developing seeds."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2018"],["dc.identifier.doi","10.1186/s13068-018-1057-4"],["dc.identifier.pmid","29507605"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15144"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59193"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","In goescholar not merged with http://resolver.sub.uni-goettingen.de/purl?gs-1/15080 but duplicate"],["dc.relation.issn","1754-6834"],["dc.rights","CC BY 4.0"],["dc.rights.access","openAccess"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","572"],["dc.title","High-level accumulation of oleyl oleate in plant seed oil by abundant supply of oleic acid substrates to efficient wax ester synthesis enzymes."],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","343"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","The ISME Journal"],["dc.bibliographiccitation.lastpage","355"],["dc.bibliographiccitation.volume","12"],["dc.contributor.author","Roitman, Sheila"],["dc.contributor.author","Hornung, Ellen"],["dc.contributor.author","Flores-Uribe, José"],["dc.contributor.author","Sharon, Itai"],["dc.contributor.author","Feussner, Ivo"],["dc.contributor.author","Béjà, Oded"],["dc.date.accessioned","2019-07-09T11:45:25Z"],["dc.date.available","2019-07-09T11:45:25Z"],["dc.date.issued","2018"],["dc.description.abstract","Cyanobacteria are among the most abundant photosynthetic organisms in the oceans; viruses infecting cyanobacteria (cyanophages) can alter cyanobacterial populations, and therefore affect the local food web and global biochemical cycles. These phages carry auxiliary metabolic genes (AMGs), which rewire various metabolic pathways in the infected host cell, resulting in increased phage fitness. Coping with stress resulting from photodamage appears to be a central necessity of cyanophages, yet the overall mechanism is poorly understood. Here we report a novel, widespread cyanophage AMG, encoding a fatty acid desaturase (FAD), found in two genotypes with distinct geographical distribution. FADs are capable of modulating the fluidity of the host's membrane, a fundamental stress response in living cells. We show that both viral FAD (vFAD) families are Δ9 lipid desaturases, catalyzing the desaturation at carbon 9 in C16 fatty acid chains. In addition, we present a comprehensive fatty acid profiling for marine cyanobacteria, which suggests a unique desaturation pathway of medium- to long-chain fatty acids no longer than C16, in accordance with the vFAD activity. Our findings suggest that cyanophages are capable of fiddling with the infected host's membranes, possibly leading to increased photoprotection and potentially enhancing viral-encoded photosynthetic proteins, resulting in a new viral metabolic network."],["dc.identifier.doi","10.1038/ismej.2017.159"],["dc.identifier.pmid","29028002"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15200"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59226"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/317184/EU//PHOTO.COMM"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/321647/EU//PHOTOPHAGE"],["dc.relation.issn","1751-7370"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.subject.ddc","572"],["dc.title","Cyanophage-encoded lipid desaturases: oceanic distribution, diversity and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","131"],["dc.bibliographiccitation.issue","S1"],["dc.bibliographiccitation.journal","Plant Biology"],["dc.bibliographiccitation.lastpage","142"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Djian, B."],["dc.contributor.author","Hornung, E."],["dc.contributor.author","Ischebeck, T."],["dc.contributor.author","Feussner, I."],["dc.date.accessioned","2019-07-09T11:49:55Z"],["dc.date.available","2019-07-09T11:49:55Z"],["dc.date.issued","2018"],["dc.description.abstract","The green microalga Lobosphaera incisa is an oleaginous eukaryotic alga that is rich in arachidonic acid (20:4). Being rich in this polyunsaturated fatty acid (PUFA), however, makes it sensitive to oxidation. In plants, lipoxygenases (LOXs) are the major enzymes that oxidise these molecules. • Here, we describe, to our best knowledge, the first characterisation of a cDNA encoding a LOX (LiLOX) from a green alga. To obtain first insights into its function, we expressed it in E. coli, purified the recombinant enzyme and analysed its enzyme activity. • The protein sequence suggests that LiLOX and plastidic LOXs from bryophytes and flowering plants may share a common ancestor. The fact that LiLOX oxidises all PUFAs tested with a consistent oxidation on the carbon n-6, suggests that PUFAs enter the substrate channel through their methyl group first (tail first). Additionally, LiLOX form the fatty acid hydroperoxide in strict S configuration. • LiLOX may represent a good model to study plastid LOX, because it is stable after heterologous expression in E. coli and highly active in vitro. Moreover, as the first characterised LOX from green microalgae, it opens the possibility to study endogenous LOX pathways in these organisms."],["dc.identifier.doi","10.1111/plb.12920"],["dc.identifier.pmid","30277010"],["dc.identifier.pmid","https://creativecommons.org/licenses/by/4.0/"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15804"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/59654"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/266401/EU//GIAVAP"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject.ddc","572"],["dc.title","The green microalga Lobosphaera incisa harbours an arachidonate 15 S‐lipoxygenase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]