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Updated: Jun 22, 2026

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
Published on: August 9, 2024
SECIS-binding protein 2, a key player in selenoprotein synthesis, is an intrinsically disordered protein
Vincent Oliéric1, Philippe Wolff, Akiko Takeuchi
1Architecture et Réactivité de l'ARN, Université de Strasbourg, CNRS, IBMC, France.
Abstract:
Selenocysteine (Sec) is co-translationally incorporated into selenoproteins at a reprogrammed UGA codon. In mammals, this requires a dedicated machinery comprising a stem-loop structure in the 3' UTR RNA (the SECIS element) and the specific SECIS Binding Protein 2. In this report, disorder-prediction methods and several biophysical techniques showed that ca. 70% of the SBP2 sequence is disordered, whereas the RNA binding domain appears to be folded and functional. These results are consistent with a recent report on the role of the Hsp90 chaperone for the folding of SBP2 and other functionally unrelated proteins bearing an RNA binding domain homologous to SBP2.
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