Publications by authors named "Jennifer Castillo Suchkou"
Nucleic Acids Res
November 2024
Article Synopsis
- The incorporation of selenocysteine (Sec) into the genetic code has led to the creation of a specialized group of proteins, known as the selenoproteome, across all life forms.*
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- In humans, the enzyme O-phosphoseryl-tRNASec selenium transferase (SepSecS) has a unique structure that limits its ability to bind more than two tRNASec molecules, due to a specific acidic α-helical extension.*
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- Research finds that the tRNA-binding mechanisms of SepSecS vary across species, with significant differences between mammals and archaea, indicating that the ability to regulate selenoprotein synthesis has evolved differently in these groups.*
Nucleic Acids Res
May 2023
Article Synopsis
- O-Phosphoseryl-tRNASec selenium transferase (SepSecS) plays a crucial role in the final step of selenocysteine synthesis in archaea and eukaryotes, highlighting its importance in maintaining the selenoproteome.
- Recent high-resolution X-ray crystallography studies reveal that the binding of tRNASec induces conformational changes in SepSecS, essential for its catalytic function, by organizing active sites and stabilizing the protein's structure.
- The formation of the productive SepSecS•tRNASec complex is driven by electrostatic interactions, providing new insights into the mechanisms behind selenocysteine formation in these organisms.
