These authors contributed equally to this work.
1521-3773/asset/2002_left.gif?v=1&s=ac6b0d94a94d7ce7a210002b8096b42feffc0bcf)
1521-3773/asset/olbannercenter.gif?v=1&s=c083e1920cd41ed129901c116018eab93b5ad3c4)
1521-3773/asset/2002_right.gif?v=1&s=451042aa3415ae3ad0729984d26dee1866aca82e)
Cover Picture
Back Cover: Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013)
Article first published online: 20 JAN 2013
DOI: 10.1002/anie.201300063
Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Aldag, C., Bröcker, M. J., Hohn, M. J., Prat, L., Hammond, G., Plummer, A. and Söll, D. (2013), Back Cover: Rewiring Translation for Elongation Factor Tu-Dependent Selenocysteine Incorporation (Angew. Chem. Int. Ed. 5/2013). Angew. Chem. Int. Ed., 52: 1596. doi: 10.1002/anie.201300063
- †
These authors contributed equally to this work.
Publication History
- Issue published online: 23 JAN 2013
- Article first published online: 20 JAN 2013
Keywords:
- genetic code;
- orthogonal translation;
- protein engineering;
- selenocysteine;
- synthetic biology
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-tRNAUTu, and EF-Tu for Sec-tRNAUTu 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.