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|style="background: #F8EABA; text-align: center;" colspan="2"||Selenocysteine|
|Molar mass||168.053 g/mol|
|style="background: #F8EABA; text-align: center;" colspan="2"|| Except where noted otherwise, data are given for|
materials in their standard state
(at 25 °C, 100 kPa)
Infobox disclaimer and references
Selenocysteine is an amino acid that is present in several enzymes (for example glutathione peroxidases, tetraiodothyronine 5' deiodinases, thioredoxin reductases, formate dehydrogenases, glycine reductases and some hydrogenases).
Selenocysteine has a structure similar to cysteine, but with an atom of selenium taking the place of the usual sulfur. Proteins that contains one or more selenocysteine residues are called selenoproteins.
Unlike other amino acids present in biological proteins, however, it is not coded for directly in the genetic code. Selenocysteine is encoded in a special way by a UGA codon, which is normally a stop codon. The UGA codon is made to encode selenocysteine by the presence of a SECIS element (SElenoCysteine Insertion Sequence) in the mRNA. The SECIS element is defined by characteristic nucleotide sequences and secondary structure base-pairing patterns. In eubacteria, the SECIS element is located immediately following the UGA codon within the reading frame for the selenoprotein. In archaea and in eukaryotes, the SECIS element is in the 3' untranslated region (3' UTR) of the mRNA, and can direct multiple UGA codons to encode selenocysteine residues. When cells are grown in the absence of selenium, translation of selenoproteins terminates at the UGA codon, resulting in a truncated, nonfunctional enzyme.
Like the other amino acids used by cells, selenocysteine has a specialized tRNA. The primary and secondary structure of selenocysteine tRNA, tRNA(Sec), differ from those of standard tRNAs in several respects, most notably in having an 8-base (bacteria) or 9-base (eukaryotes) pair acceptor stem, a long variable region arm, and substitutions at several well-conserved base positions. The selenocysteine tRNAs are initially charged with serine by seryl-tRNA ligase, but the resulting Ser-tRNA(Sec) is not used for translation because it is not recognised by the normal translation factor (EF-Tu in bacteria, EF1-alpha in eukaryotes). Rather, the tRNA-bound seryl residue is converted to a selenocysteyl-residue by the pyridoxal phosphate-containing enzyme selenocysteine synthase. Finally, the resulting Sec-tRNA(Sec) is specifically bound to an alternative translational elongation factor (SelB or mSelB) which delivers it in a targeted manner to the ribosomes translating mRNAs for selenoproteins. The specificity of this delivery mechanism is brought about by the presence of an extra protein domain (in bacterial SelB) or an extra subunit (SBP-2 for eukaryotic mSelB) which bind to the corresponding RNA secondary structures formed by the SecIS elements in selenoprotein mRNAs. The SecIS elements of bacterial selenoproteins (as far as analysed) are located within the coding sequences immediately following the UGA codons for selenocysteine, those of Eukarya and Archaea are located in the 3' UTR of the respective mRNAs. In addition, at least one case has been described for an archaeal selenoprotein mRNA containing its SecIS in the 5' UTR.
- ↑ IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN) and Nomenclature Committee of IUBMB (NC-IUBMB) (1999). Newsletter 1999. European Journal of Biochemistry 264 (2): 607-609.
- F. Zinoni, A. Birkmann, T. C. Stadtman and A. Bock (1986). Nucleotide Sequence and Expression of the Selenocysteine-Containing Polypeptide of Formate Dehydrogenase (Formate-hydrogen-lyase-Linked) from Escherichia coli. PNAS 83 (13): 4650-4654.
- F. Zinoni, A. Birkmann, W. Leinfelder and A. Bock (1987). Cotranslational Insertion of Selenocysteine into Formate Dehydrogenase from Escherichia coli Directed by a UGA Codon. PNAS 84 (10): 3156-3160.
- Boyce E. Cone, Rafael Martin Del Rio, Joe Nathan Davis, and Thressa C. Stadtman (1976). Chemical Characterization of the Selenoprotein Component of Clostridial Glycine Reductase: Identification of Selenocysteine as the Organoselenium Moiety. PNAS 73 (8): 2659-2663.
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