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Threading the needle: getting selenocysteine into proteins.


ABSTRACT: The co-translational incorporation of selenocysteine (Sec) requires that UGA be recognized as a sense rather than a nonsense codon. This is accomplished by the concerted action of a Sec insertion sequence (SECIS) element, SECIS binding protein 2, and a ternary complex of the Sec specific elongation factor, Sec-tRNA(Sec), and GTP. The mechanism by which they alter the canonical protein synthesis reaction has been elusive. Here we present an overview of the mechanistic perspective on Sec incorporation, highlighting recent advances in the field.

SUBMITTER: Donovan J 

PROVIDER: S-EPMC2864665 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Threading the needle: getting selenocysteine into proteins.

Donovan Jesse J   Copeland Paul R PR  

Antioxidants & redox signaling 20100401 7


The co-translational incorporation of selenocysteine (Sec) requires that UGA be recognized as a sense rather than a nonsense codon. This is accomplished by the concerted action of a Sec insertion sequence (SECIS) element, SECIS binding protein 2, and a ternary complex of the Sec specific elongation factor, Sec-tRNA(Sec), and GTP. The mechanism by which they alter the canonical protein synthesis reaction has been elusive. Here we present an overview of the mechanistic perspective on Sec incorpora  ...[more]

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