A5027465749- Redox biology and oxidative stress
- Photosynthetic Processes and Mechanisms
- Glutathione Transferases and Polymorphisms
- Plant Stress Responses and Tolerance
- Plant responses to water stress
- Genomics, phytochemicals, and oxidative stress
- Mitochondrial Function and Pathology
- Heat shock proteins research
- Sulfur Compounds in Biology
- Insect and Pesticide Research
- Plant Micronutrient Interactions and Effects
- ATP Synthase and ATPases Research
- Metal-Catalyzed Oxygenation Mechanisms
- Trace Elements in Health
- thermodynamics and calorimetric analyses
- Plant nutrient uptake and metabolism
Bielefeld University
2016-2021
Thiol-dependent redox regulation controls central processes in plant cells including photosynthesis. Thioredoxins reductively activate, for example, Calvin-Benson cycle enzymes. However, the mechanism of oxidative inactivation is unknown despite its importance efficient regulation. Here, abundant 2-cysteine peroxiredoxin (2-CysPrx), but not site-directed variants, mediates rapid activated fructose-1,6-bisphosphatase and NADPH-dependent malate dehydrogenase (MDH) presence proper thioredoxins....
The integration of redox- and reactive oxygen species-dependent signaling metabolic activities is fundamental to plant acclimation biotic abiotic stresses. Previous data suggest the existence a dynamically interacting module in chloroplast stroma consisting cyclophilin 20-3 (Cyp20-3), O-acetylserine(thiol)lyase B (OASTL-B), 2-cysteine peroxiredoxins A/B (2-CysPrx) serine acetyltransferase 2;1 (SERAT2;1). functionality this COPS influenced by redox stimuli oxophytodienoic acid (OPDA), which...
2-Cysteine peroxiredoxins (2-CysPRX) are highly abundant thiol peroxidases in chloroplasts and play key roles reactive oxygen species (ROS) defense redox signaling. Peroxide-dependent oxidation of cysteines induces conformational changes that alter the ability for protein-protein interactions. For regeneration, 2-CysPRXs withdraw electrons from thioredoxins (TRXs) participate redox-dependent regulation by affecting state TRX-dependent targets, example, chloroplast metabolism. This work...
Protein oligomerization is central to biological function and regulation, yet its experimental quantification measurement of dynamic transitions in solution remain challenging. Here, we show that single molecule mass photometry quantifies affinity polydispersity heterogeneous protein complexes solution. We demonstrate these capabilities by studying the functionally relevant oligomeric equilibria 2-cysteine peroxiredoxins (2CPs). Comparison plant human 2CPs as a concentration redox state...
2-Cysteine peroxiredoxins (2-CysPrxs) switch between functions as a thiol peroxidase, chaperone, an interaction partner and possibly proximity-based oxidase in redox-dependent manner. In photosynthetic eukaryotes, 2-CysPrx localizes to the plastid, context of photosynthesis enables ascorbate peroxidase-independent water–water cycle for detoxifying H2O2. The high degree evolutionary conservation suggests that switching is essential characteristic needed transduce redox information downstream...
The chloroplast primary metabolism is of central importance for plant growth and performance. Therefore, it tightly regulated in order to adequately respond multiple environmental conditions. A major fluctuation that plants experience each day the change between night, i.e., assimilation dissimilation. Among other mechanisms, thioredoxin-mediated redox regulation an important component plastid-localized metabolic enzymes. While assimilatory processes such as Calvin–Benson cycle are activated...
Secondary active transporters are driven by the proton motif force which is generated primary such as vacuolar pumps V-ATPase and V-PPase. The vacuole occupies up to 90 % of mature cell acidification lumen a challenging energy-consuming task for plant cell. Therefore, direct coupling secondary expected enhance transport efficiency reduce energy consumption processes across tonoplast. This has been addressed analyzing physical functional interactions between selection including pump AVP1,...
Abstract Single molecule mass photometry was used to study the dynamic equilibria of ubiquitous and highly abundant 2-Cysteine peroxiredoxins (2-CysPRX). 2-CysPRXs adopt distinct functions in all cells dependent on their oligomeric conformation ranging from dimers decamers high molecular weight aggregates (HMW). The state depends redox catalytic cysteinyl residues. To which degree they interconvert, how interconversion is regulated, oligomerisation propensity organism specific remains,...
Abstract Thiol-dependent redox regulation controls central processes in plant cells including photosynthesis. Thioredoxins reductively activate e.g. Calvin-Benson cycle enzymes. However the mechanism of oxidative inactivation is unknown despite its importance for efficient regulation. Here, abundant 2-cysteine peroxiredoxin (2-CysPrx), but not site-directed variants, mediates rapid activated fructose-1,6-bisphosphatase and NADPH-dependent malate dehydrogenase (MDH) presence proper...