Decoding apparatus for eukaryotic selenocysteine insertion
Open Access
- 1 August 2000
- journal article
- research article
- Published by Springer Nature in EMBO Reports
- Vol. 1 (2) , 158-163
- https://doi.org/10.1093/embo-reports/kvd033
Abstract
Decoding UGA as selenocysteine requires a unique tRNA, a specialized elongation factor, and specific secondary structures in the mRNA, termed SECIS elements. Eukaryotic SECIS elements are found in the 3′ untranslated region of selenoprotein mRNAs while those in prokaryotes occur immediately downstream of UGA. Consequently, a single eukaryotic SECIS element can serve multiple UGA codons, whereas prokaryotic SECIS elements only function for the adjacent UGA, suggesting distinct mechanisms for recoding in the two kingdoms. We have identified and characterized the first eukaryotic selenocysteyl‐tRNA‐specific elongation factor. This factor forms a complex with mammalian SECIS binding protein 2, and these two components function together in selenocysteine incorporation in mammalian cells. Expression of the two functional domains of the bacterial elongation factor–SECIS binding protein as two separate proteins in eukaryotes suggests a mechanism for rapid exchange of charged for uncharged selenocysteyl‐tRNA–elongation factor complex, allowing a single SECIS element to serve multiple UGA codons.Keywords
This publication has 24 references indexed in Scilit:
- Selenoprotein P Expression, Purification, and Immunochemical CharacterizationJournal of Biological Chemistry, 2000
- A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAsThe EMBO Journal, 2000
- Functional Interaction of Mammalian Valyl-tRNA Synthetase with Elongation Factor EF-1α in the Complex with EF-1HPublished by Elsevier ,1999
- Structural model for the selenocysteine-specific elongation factor SelBBiochimie, 1996
- Domain Structure of the Prokaryotic Selenocysteine-specific Elongation Factor SelBJournal of Molecular Biology, 1996
- A channeled tRNA cycle during mammalian protein synthesis.Proceedings of the National Academy of Sciences, 1995
- Recognition of UGA as a selenocysteine codon in Type I deiodinase requires sequences in the 3′ untranslated regionNature, 1991
- Type I iodothyronine deiodinase is a selenocysteine-containing enzymeNature, 1991
- Identification of a novel translation factor necessary for the incorporation of selenocysteine into proteinNature, 1989
- Aminoacyl-transfer RNA populations in mammalian cells. Chromatographic profiles and patterns of codon recognitionBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1979