Communication

Decoding the Logic of the tRNA Regiospecificity of Nonribosomal FemXWv Aminoacyl Transferase†

  1. Matthieu Fonvielle Dr.1,‡,
  2. Maryline Chemama Dr.2,‡,
  3. Maxime Lecerf1,
  4. Régis Villet Dr.1,
  5. Patricia Busca Dr.2,
  6. Ahmed Bouhss Dr.3,
  7. Mélanie Ethève-Quelquejeu Dr.2,
  8. Michel Arthur Dr.1

Article first published online: 22 JUN 2010

DOI: 10.1002/anie.201001473

Issue

Angewandte Chemie International Edition

Angewandte Chemie International Edition

Volume 49, Issue 30, pages 5115–5119, July 12, 2010

Additional Information

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

Author Information

  1. 1

    Laboratoire de Recherche Moléculaire sur les Antibiotiques, Centre de Recherche des Cordeliers, Equipe 12, UMR S 872, INSERM, Université Pierre et Marie Curie—Paris 6 and Université Paris Descartes, 15, rue de l'Ecole de Médecine, 75006 Paris (France), Fax: (+33) 1-4325-6812

  2. 2

    Institut Parisien de Chimie Moléculaire, CNRS UMR 7201, Université Pierre et Marie Curie—Paris 6, 4, place Jussieu, 75005 Paris (France), Fax: (+33) 1-4427-5504

  3. 3

    Laboratoire des Enveloppes Bactériennes et Antibiotiques, Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, UMR 8619, CNRS, Université Paris-Sud, 91405 Orsay (France)

  1. ‡

    These authors contributed equally to this work.

  1. †

    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.

  2. ‡

    These authors contributed equally to this work.

Publication History

  1. Issue published online: 7 JUL 2010
  2. Article first published online: 22 JUN 2010
  3. Manuscript Received: 11 MAR 2010

Funded by

  • European Community
  • Fondation Recherche Médicale

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Keywords:

  • enzyme catalysis;
  • peptides;
  • transesterification;
  • transferases;
  • tRNA mimics
Thumbnail image of graphical abstract

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).

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