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Updated: Jul 1, 2026

Utilizing Thermal Shift Assay to Probe Substrate Binding to Selenoprotein O
Published on: August 9, 2024
Evolutionary and Biochemical Perspectives on the Incorporation and Utilization of Selenocysteine
Mihajlo Stašuk1, Jesse Donovan2, Paul R Copeland3
1Department of Genetics, Microbiology and Statistics, Universitat de Barcelona, Barcelona, Catalonia 08028, Spain.
Abstract:
Selenocysteine (Sec) incorporation is a uniquely complex and essential form of ribosomal recoding that redefines in-frame UGA codons through an evolutionarily ancient apparatus. Eukaryotic selenoprotein biosynthesis requires a specialized tRNA as well as elongation and selenium-donor factors, and incorporation depends on a 3' untranslated region (UTR) RNA structure, the Sec insertion sequence (SECIS) element. The SECIS is recognized by SECIS-binding protein 2 (SECISBP2/SBP2), resulting in recruitment of the Sec-specific elongation factor eEFSec. Here, we delve into the evolutionary and biochemical basis for Sec incorporation in eukaryotes, summarizing the current understanding of the cis and trans determinants that tune this form of recoding.
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