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Journal of Bacteriology, May 2007, p. 3927-3931, Vol. 189, No. 10
0021-9193/07/$08.00+0 doi:10.1128/JB.00084-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Lionel Dubost,5
Martine Fourgeaud,1,2,3
Jean-Luc Mainardi,1,2,3,4
Sébastien Petit-Frère,1,2,3
Arul Marie,5
Dominique Mengin-Lecreulx,6
Michel Arthur,1,2,3 and
Laurent Gutmann1,2,3,4
INSERM, U655-LRMA, Paris, F-75006 France,1 Université Pierre et Marie Curie-Paris 6, Centre de Recherches Biomédicales des Cordeliers, Paris, F-75006 France,2 Université Paris-Descartes, Faculté de Médecine René Descartes, Centre de Recherches Biomédicales des Cordeliers, Paris, F-75006 France,3 AP-HP, Hôpital Européen Georges Pompidou, Paris, F-75015 France,4 Muséum National d'Histoire Naturelle, Plateforme de Spectrométrie de Masse et de Protéomique, Département Recherche Développement et Diversité Moléculaire, Paris, F-75005 France,5 Laboratoire des Enveloppes Bactériennes et Antibiotiques, UMR 8619 CNRS, Université Paris-Sud, 91405 Orsay, France6
Received 16 January 2007/ Accepted 9 March 2007
The L,D-transpeptidase Ldtfm catalyzes peptidoglycan cross-linking in ß-lactam-resistant mutant strains of Enterococcus faecium. Here, we show that in Escherichia coli Ldtfm homologues are responsible for the attachment of the Braun lipoprotein to murein, indicating that evolutionarily related domains have been tailored to use muropeptides or proteins as acyl acceptors in the L,D-transpeptidation reaction.
Published ahead of print on 16 March 2007.
Present address: INSERM U781, Hôpital Necker Enfants Malades, 75015, Paris, France.
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