Rewiring Translation for Elongation Factor Tu‐Dependent Selenocysteine Incorporation1. Issue 5 (27th November 2012)

• 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: 1441
• Page End: 1445
• Publication Date: 2012-11-27
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201207567
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Enjoying UTu in concert</bold>: A synthetic tRNA (tRNA^UTu) was used as a substrate for three <italic>E. coli</italic> proteins: seryl‐tRNA synthetase (SerRS) forming Ser‐tRNA^UTu, selenocysteine (Sec) synthase (SelA) generating Sec‐tRNA^UTu, and EF‐Tu for Sec‐tRNA^UTu transport to the ribosome (see scheme). tRNA^UTu can be used by the ribosome, thus allowing site‐specific Sec insertion into proteins, including formate dehydrogenase H, selenoglutaredoxin, and glutathione peroxidase.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg1p8rs4zq" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>