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Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl‐tRNA formation systems
Author(s) -
Yuan Jing,
O'Donoghue Patrick,
Ambrogelly Alex,
Gundllapalli Sarath,
Sherrer R. Lynn,
Palioura Sotiria,
Simonović Miljan,
Söll Dieter
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.11.005
Subject(s) - selenocysteine , genetic code , transfer rna , stop codon , amino acid , biology , protein biosynthesis , biochemistry , translation (biology) , rna , genetics , chemistry , gene , messenger rna , enzyme , cysteine
Selenocysteine and pyrrolysine, known as the 21st and 22nd amino acids, are directly inserted into growing polypeptides during translation. Selenocysteine is synthesized via a tRNA‐dependent pathway and decodes UGA (opal) codons. The incorporation of selenocysteine requires the concerted action of specific RNA and protein elements. In contrast, pyrrolysine is ligated directly to tRNA Pyl and inserted into proteins in response to UAG (amber) codons without the need for complex re‐coding machinery. Here we review the latest updates on the structure and mechanisms of molecules involved in Sec‐tRNA Sec and Pyl‐tRNA Pyl formation as well as the distribution of the Pyl‐decoding trait.