These authors contributed equally to this work.
Decoding the Logic of the tRNA Regiospecificity of Nonribosomal FemXWv Aminoacyl Transferase†
Article first published online: 22 JUN 2010
Copyright © 2010 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 49, Issue 30, pages 5115–5119, July 12, 2010
How to Cite
Fonvielle, M., Chemama, M., Lecerf, M., Villet, R., Busca, P., Bouhss, A., Ethève-Quelquejeu, M. and Arthur, M. (2010), Decoding the Logic of the tRNA Regiospecificity of Nonribosomal FemXWv Aminoacyl Transferase. Angew. Chem. Int. Ed., 49: 5115–5119. doi: 10.1002/anie.201001473
This research was supported by the European Community (EUR-INTAFAR, Project No. LSHM-CT-2004-512138, 6th PCRD) and by the Fondation Recherche Médicale (“fin de thèse” to R.V. and M.C.). FemXWv is the FemX alanyl transferase of Weissella viridescens.
- Issue published online: 7 JUL 2010
- Article first published online: 22 JUN 2010
- Manuscript Received: 11 MAR 2010
- European Community
- Fondation Recherche Médicale
- enzyme catalysis;
- tRNA mimics
Natural selection: Replacement of the 3′-OH group of Ala-tRNAAla with 3′-H affected FemXWv-catalyzed aminoacyl transfer from the 2′-position, but not substrate binding. The ability of FemXWv to bind and transacylate the 3′-O-Ala isomer initially formed by alanyl-tRNA synthetase (AlaRS) may be crucial for efficient competition with the ribosome (see scheme).