Back Cover: Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013). Issue 5 (20th January 2013)

• Record Type: Journal Article
• Authors: Aldag, Caroline; Bröcker, Markus J.; Hohn, Michael J.; Prat, Laure; Hammond, Gifty; Plummer, Abigail; Söll, Dieter
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 5(2013)
• Page Start: 1596
• Page End: 1596
• Publication Date: 2013-01-20
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201300063
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Synthetic tRNA for selenoprotein production</bold> is described by D. Söll et al. in their Communication on <ext-link ext-link-type="doi" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink">page 1441 ff.</ext-link> The tRNA is a substrate for three <italic>E. coli</italic> 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.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p8rs48p" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>