23 research outputs found
Die Missionskonzeption Franz Michael Zahns (1862-1900) : Überlegungen zur epistemischen Dimension der kolonialen Begegnungen in Togo
No full textAn epistemology of colonialism using the example of the mission concept of the NMG mission inspector Franz Michael Zahn, who died in 1900. The author analyses the effects of missionary work in South Togo and refers to the discourse theory of Michael Foucault. In the dissertation, the investigation of colonial power takes the form of a moral-critical analysis with a focus on the concept of "colonial ethics". The author summarized missionary or colonial knowledge understood as knowledge of (Christian) governmental practice (colonial governmentality) with the concept of morality and, for colonial historiography, shapes the new object of analysis of the "moral discourse".
Eine Epistemologie des Kolonialismus am Beispiel der Missionskonzeption von dem im Jahre 1900 verstorbenen Missionsinspektor der NMG Franz Michael Zahn. Der Autor analysiert die Auswirkungen der Missionierung im Süd-Togo und bezieht sich dabei auf die Diskurstheorie von Michael Foucault. Die Untersuchung der Kolonialmacht nimmt in der Dissertation die Form einer moralkritischen Analyse mit Fokus auf den Begriff der "Kolonialethik". Das Missions-bzw. Kolonialwissen verstanden als ein Wissen der (christlichen) Regierungspraxis (koloniale Gouvernementalität) fasste der Autor mit dem Moralbegriff zusammen und prägt für die Kolonialgeschichtschreibung den neuen Analysegegenstand des "Moraldiskurses"
Identification of cis-active elements in U. maydis mig2 promoters conferring high-level activity during pathogenic growth in maize
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The Ustilago maydis a2 Mating-Type Locus Genes lga2 and rga2 Compromise Pathogenicity in the Absence of the Mitochondrial p32 Family Protein Mrb1.
No full textThe Ustilago maydis mrb1 gene specifies a mitochondrial matrix protein with significant similarity to mitochondrial p32 family proteins known from human and many other eukaryotic species. Compatible mrb1 mutant strains were able to mate and form dikaryotic hyphae; however, proliferation within infected tissue and the ability to induce tumor development of infected maize (Zea mays) plants were drastically impaired. Surprisingly, manifestation of the mrb1 mutant phenotype selectively depended on the a2 mating type locus. The a2 locus contains, in addition to pheromone signaling components, the genes lga2 and rga2 of unknown function. Deletion of lga2 in an a2Deltamrb1 strain fully restored pathogenicity, whereas pathogenicity was partially regained in an a2Deltamrb1Deltarga2 strain, implicating a concerted action between Lga2 and Rga2 in compromising pathogenicity in Deltamrb1 strains. Lga2 and Rga2 localized to mitochondria and Mrb1 interacted with Rga2 in the yeast two-hybrid system. Conditional expression of lga2 in haploid cells reduced vegetative growth, conferred mitochondrial fragmentation and mitochondrial DNA degradation, and interfered with respiratory activity. The consequences of lga2 overexpression depended on the expression strength and were greatly exacerbated in Deltamrb1 mutants. We propose that Lga2 interferes with mitochondrial fusion and that Mrb1 controls this activity, emphasizing a critical link between mitochondrial morphology and pathogenicity
‐type zinc finger transcription factor Mzr1 regulates fungal gene expression during the biotrophic growth stage
No full textTORC1 Determines Fab1 Lipid Kinase Function at Signaling Endosomes and Vacuoles
No full textOrganelles of the endomembrane system maintain their identity and integrity during growth or stress conditions by homeostatic mechanisms that regulate membrane flux and biogenesis. At lysosomes and endosomes, the Fab1 lipid kinase complex and the nutrient-regulated target of rapamycin complex 1 (TORC1) control the integrity of the endolysosomal homeostasis and cellular metabolism. Both complexes are functionally connected as Fab1-dependent generation of PI(3,5)P2 supports TORC1 activity. Here, we identify Fab1 as a target of TORC1 on signaling endosomes, which are distinct from multivesicular bodies, and provide mechanistic insight into their crosstalk. Accordingly, TORC1 can phosphorylate Fab1 proximal to its PI3P-interacting FYVE domain, which causes Fab1 to shift to signaling endosomes, where it generates PI(3,5)P2. This, in turn, regulates (1) vacuole morphology, (2) recruitment of TORC1 and the TORC1-regulatory Rag GTPase-containing EGO complex to signaling endosomes, and (3) TORC1 activity. Thus, our study unravels a regulatory feedback loop between TORC1 and the Fab1 complex that controls signaling at endolysosomes.sponsorship: We thank Lars Langemeyer for feedback, all members from the Ungermann lab for discussions, and Kathrin Auffarth, Angela Perz, and Malika Jaquenoud for expert technical assistance. This work was supported by the DFG (UN111/10-1 to C.U.), the Canton of Fribourg (to J.D. and C.D.V.), and the Swiss National Science Foundation (310030_166474/184671 to C.D.V. and 310030_184781 and 316030_177088 to J.D.). Z.C. received support from a travel stipend of the Boehringer Ingelheim Fonds. P.C.M. received additional support from the graduate program of the Collaborative Research Center 944 (SFB 944) and Department of Biology/Chemistry Osnabruck. E.E. received a fellowship of FWO Vlaanderen, Belgium (SB-FWO 1S06419N). (DFG|UN111/10-1, Canton of Fribourg, Swiss National Science Foundation|310030_166474/184671, Swiss National Science Foundation|310030_184781, Swiss National Science Foundation|316030_177088, Boehringer Ingelheim Fonds, graduate program of the Collaborative Research Center 944|SFB 944, Department of Biology/Chemistry Osnabruck, FWO Vlaanderen, Belgium|SB-FWO 1S06419N, MRC|MC_UU_00012/6, Swiss National Science Foundation (SNF)|310030_166474, Swiss National Science Foundation (SNF)|310030_184781, Swiss National Science Foundation (SNF)|316030_177088, Medical Research Council|MC_UU_00012/6)status: Publishe
Comparison of Minimally Invasive XEN45 Gel Stent Implantation in Glaucoma Patients Without and With Prior Interventional Therapies
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AP‐3 vesicle uncoating occurs after HOPS‐dependent vacuole tethering
No full textHeterotetrameric adapter (AP) complexes cooperate with the smallGTPase Arf1 or lipids in cargo selection, vesicle formation, and budding at endomembranes in eukaryotic cells. While mostAPcomplexes also require clathrin as the outer vesicle shell, formation ofAP-3-coated vesicles involved in Golgi-to-vacuole transport in yeast has been postulated to depend on Vps41, a subunit of the vacuolarHOPStethering complex.HOPShas also been identified as the tether ofAP-3 vesicles on vacuoles. To unravel this conundrum of a dual Vps41 function, we anchored Vps41 stably to the mitochondrial outer membrane. By monitoringAP-3 recruitment, we now show that Vps41 can tetherAP-3 vesicles to mitochondria, yetAP-3 vesicles can form in the absence of Vps41 or clathrin. By proximity labeling and mass spectrometry, we identify the Arf1GTPase-activating protein (GAP) Age2 at theAP-3 coat and show that tethering, but not fusion at the vacuole can occur without complete uncoating. We conclude thatAP-3 vesicles retain their coat after budding and that their complete uncoating occurs only after tethering at the vacuole.</p
Vps41 functions as a molecular ruler for HOPS tethering complex-mediated membrane fusion
No full textFusion at the lysosome (or the yeast vacuole) requires the conserved hexameric HOPS tethering complex. In the yeast Saccharomyces cerevisiae, HOPS binds to the vacuolar Rab7-like GTPase Ypt7 via its subunits Vps41 and Vps39 and supports fusion by promoting SNARE assembly. In contrast to its sister complex CORVET, the Ypt7-interacting domain of Vps41 in the HOPS complex is connected to the core by a long, extended α-solenoid domain. Here, we show that this solenoid acts as a molecular ruler to position the Ypt7-interacting region of Vps41 relative to the core of HOPS to support function. Mutant complexes with a shortened or extended α-solenoid region in Vps41 still tethered membranes, but failed to efficiently support their fusion. In vivo, Vps41 mutants grew poorly and showed defects in vacuolar morphology, endolysosomal sorting and autophagy. Importantly, when a length-compensating linker was inserted instead of the shortened α-solenoid domain, these defects were rescued. This suggests that the Rab-specific Vps41 subunit requires the exact length of the α-solenoid domain but not the α-solenoid architecture for functionality, suggesting a revised model of how HOPS supports fusion.</p
