Unique features of selenocysteine incorporation function within the context of general eukaryotic translational processes. (26th October 2005)

• Record Type: Journal Article
• Authors: Small-Howard, A.L.; Berry, M.J.
• Is Part Of: Biochemical Society transactions. Volume 33:Number 6(2005)
• Page Start: 1493
• Page End: 1497
• Publication Date: 2005-10-26
• Subjects: EFsec -- nonsense-mediated decay (NMD) -- selenocysteine -- selenocysteine biosynthesis -- selenocysteine insertion sequence-binding protein 2 (SPB2) -- translational process; Biochemistry -- Congresses; 572
• DOI: 10.1042/BST0331493
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Unlike other essential dietary trace elements, selenium exerts its biological actions through its direct incorporation into selenoproteins, as a part of the 21st amino acid, selenocysteine. Fundamental studies have elucidated the unique structures and putative functions of multiple co-translational factors required for the incorporation of selenocysteine into selenoproteins. The current challenge is to understand how these selenocysteine incorporation factors function within the framework of translation. In eukaryotes, co-ordinating nuclear transcription with cytoplasmic translation of genes is a challenge involving complex spatial and temporal regulation. Selenoproteins utilize the common cellular machinery required for synthesis of non-selenoproteins. This machinery includes the elements involved in transcription, mRNA splicing and transport, and translational processes. Many investigators have emphasized the differences between the expression of selenoproteins and other eukaryotic proteins, whereas this review will attempt to highlight common themes and point out where additional interactions may be discovered.