Work

Threading the Needle: Getting Selenocysteine Into Proteins

Year: 2009

Type: review

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.

Source: Antioxidants and Redox Signaling

DOI: 10.1089/ars.2009.2878

Authors: Jesse Donovan, Paul R. Copeland

Institution: University of Medicine and Dentistry of New Jersey

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: National Institute of General Medical Sciences

Awards: The translational control of selenoprotein synthesis, Functional analysis of SBP2 and selenocysteine incorporation