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Back Cover: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013)
Author(s) -
Aldag Caroline,
Bröcker Markus J.,
Hohn Michael J.,
Prat Laure,
Hammond Gifty,
Plummer Abigail,
Söll Dieter
Publication year - 2013
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201300063
Subject(s) - selenocysteine , ribosome , ef tu , transfer rna , elongation factor , translation (biology) , protein biosynthesis , chemistry , biochemistry , cover (algebra) , selenoprotein , biology , enzyme , rna , messenger rna , gene , mechanical engineering , glutathione , glutathione peroxidase , cysteine , engineering
Synthetic tRNA for selenoprotein production is described by D. Söll et al. in their Communication on page 1441 ff. The tRNA is a substrate for three E. coli proteins: seryl‐tRNA synthetase (SerRS), selenocysteine synthase (SelA) generating Sec‐tRNA UTu , and EF‐Tu for Sec‐tRNA UTu transport to the ribosome, which allows site‐specific Sec insertion into proteins. This system has general utility in protein engineering, molecular biology, and disease research.