Biosynthesis, Engineering, and Delivery of Selenoproteins

Selenocysteine (Sec) was discovered as the 21st genetically encoded amino acid. In nature, site-directed incorporation of Sec into proteins requires specialized biosynthesis and recoding machinery that evolved distinctly in bacteria compared to archaea and eukaryotes. Many organisms, including highe...

Full description

Saved in:
Bibliographic Details
Published in:International journal of molecular sciences 2023-12, Vol.25 (1), p.223
Main Authors: Wright, David E, O'Donoghue, Patrick
Format: Article
Language:English
Subjects:
amber codon
Amino Acids
aminoacyl-tRNA synthetases
Animals
Antifibrinolytic Agents
Archaea
Auranofin
Bacteria
Biosynthesis
Cells
Comparative analysis
Deoxyribonucleic acid
DNA
elongation factor
Enzymes
Genes
genetic code expansion
Humans
Incorporation
Invertebrates
Kinases
Mammals
opal codon
Polypeptides
Protein synthesis
Proteins
Review
Ribonucleic acid
RNA
Saccharomyces cerevisiae
selenocysteine
Selenocysteine - genetics
Selenoproteins - genetics
Transfer RNA
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Selenocysteine (Sec) was discovered as the 21st genetically encoded amino acid. In nature, site-directed incorporation of Sec into proteins requires specialized biosynthesis and recoding machinery that evolved distinctly in bacteria compared to archaea and eukaryotes. Many organisms, including higher plants and most fungi, lack the Sec-decoding trait. We review the discovery of Sec and its role in redox enzymes that are essential to human health and important targets in disease. We highlight recent genetic code expansion efforts to engineer site-directed incorporation of Sec in bacteria and yeast. We also review methods to produce selenoproteins with 21 or more amino acids and approaches to delivering recombinant selenoproteins to mammalian cells as new applications for selenoproteins in synthetic biology.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms25010223