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TrypOx, a novel eukaryotic homologue of the redox-regulated chaperone Hsp33 in Trypanosoma brucei

ABSTRACT: In this study, we describe a novel eukaryotic homologue of Hsp33 in Trypanosoma brucei.Bioinformatics analysis of the Hsp33 family suggested that eukaryotic pathogens belonging to the kinetoplastids, such as Trypanosoma cruzi,Trypanosoma brucei spp, and leishmaniasis had persevered Hsp33 homologues in their genomes. We showed that RNAi silencing of TrypOx led to a significant decrease in the survival of T.brucei under mild oxidative stress conditions,and then we adopted a proteomics-driven approach to investigatethe role of TrypOx in defining the oxidative stress response. Our results showed that depletion of TrypOx significantly altered the abundance of proteins mediating redox homeostasis,linking TrypOx with the antioxidant system and implying a protetcive role of Trypox against oxidative stress.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Trypanosoma Brucei

SUBMITTER: Samar Aramin

LAB HEAD: Dana Reichmann

PROVIDER: PXD018965 | Pride | 2020-07-28

REPOSITORIES: Pride

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Project description:This is the model with unfitted parameters described in the article Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress Markus Ralser, Mirjam M Wamelink, Axel Kowald, Birgit Gerisch, Gino Heeren, Eduard A Struys, Edda Klipp, Cornelis Jakobs, Michael Breitenbach, Hans Lehrach and Sylvia Krobitsch, J Biol 2007 6(4):10; PMID: 18154684 , doi: 10.1186/jbiol61 Abstract: BACKGROUND: Eukaryotic cells have evolved various response mechanisms to counteract the deleterious consequences of oxidative stress. Among these processes, metabolic alterations seem to play an important role. RESULTS: We recently discovered that yeast cells with reduced activity of the key glycolytic enzyme triosephosphate isomerase exhibit an increased resistance to the thiol-oxidizing reagent diamide. Here we show that this phenotype is conserved in Caenorhabditis elegans and that the underlying mechanism is based on a redirection of the metabolic flux from glycolysis to the pentose phosphate pathway, altering the redox equilibrium of the cytoplasmic NADP(H) pool. Remarkably, another key glycolytic enzyme, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), is known to be inactivated in response to various oxidant treatments, and we show that this provokes a similar redirection of the metabolic flux. CONCLUSION: The naturally occurring inactivation of GAPDH functions as a metabolic switch for rerouting the carbohydrate flux to counteract oxidative stress. As a consequence, altering the homoeostasis of cytoplasmic metabolites is a fundamental mechanism for balancing the redox state of eukaryotic cells under stress conditions. Different realtive enzyme velocities can be simulated by varying the parameters k_rel_TPI and k_rel_GAPDH . This model originates from BioModels Database: A Database of Annotated Published Models. It is copyright (c) 2005-2010 The BioModels Team. For more information see the terms of use . To cite BioModels Database, please use Le Novère N., Bornstein B., Broicher A., Courtot M., Donizelli M., Dharuri H., Li L., Sauro H., Schilstra M., Shapiro B., Snoep J.L., Hucka M. (2006) BioModels Database: A Free, Centralized Database of Curated, Published, Quantitative Kinetic Models of Biochemical and Cellular Systems Nucleic Acids Res., 34: D689-D691.

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TrypOx, a novel eukaryotic homologue of the redox-regulated chaperone Hsp33 in Trypanosoma brucei

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