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Updated: May 31, 2026

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
Published on: August 9, 2024
Oxidative stress protection of Trypanosomes requires selenophosphate synthase
F C Costa1, M A V Oliva, T C L de Jesus
1Laboratory of Protein Crystallography and Structural Biology, Physics Institute of São Carlos, University of São Paulo, Brazil.
Abstract:
Selenoproteins are characterized by the incorporation of at least one amino acid selenocysteine (Sec-U) encoded by in-frame UGA stop codons. These proteins, as well as the components of the Sec synthesis pathway, are present in members of the bacteria, archaea and eukaryote domains. Although not a ubiquitous pathway in all organisms, it was also identified in several protozoa, including the Kinetoplastida. Genetic evidence has indicated that the pathway is non-essential to the survival of Trypanosoma growing in non-stressed conditions. By analyzing the effects of RNA interference of the Trypanosoma brucei selenophosphate synthetase SPS2, we found a requirement under sub-optimal growth conditions. The present work shows that SPS2 is involved in oxidative stress protection of the parasite and its absence severely hampers the parasite survival in the presence of an oxidizing environment that results in an apoptotic-like phenotype and cell death.
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