Abstract
AbstractPeroxiredoxins (Prxs) are crucially involved in maintaining intracellular H2O2homeostasis via their peroxidase activity. However, more recently, this class of proteins was found to also transmit oxidizing equivalents to selected downstream proteins, which suggests an important function of Prxs in the regulation of cellular protein redox relays. Using a pull-down assay based on mixed disulfide fishing, we characterized the thiol-dependent interactome of cytosolic Prx1a and mitochondrial Prx1m from the apicomplexan malaria parasitePlasmodium falciparum(Pf). Here, 127 cytosolic and 20 mitochondrial proteins that are components of essential cellular processes were found to interact withPfPrx1a andPfPrx1m, respectively. Notably, our data obtained with active-site mutants suggests that reducing equivalents might also be transferred from Prxs to target proteins. Initial functional analyses indicated that the interaction with Prx can strongly impact the activity of target proteins. The results provide initial insights into the interactome of Prxs at the level of a eukaryotic whole cell proteome. Furthermore, they contribute to our understanding of redox regulatory principles and thiol-dependent redox relays of Prxs in subcellular compartments.
Funder
LOEWE Centre DRUID
Deutsche Forschungsgemeinschaft
Publisher
Springer Science and Business Media LLC
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