Previous Article | Next Article ![]()
Journal of Bacteriology, June 2007, p. 4332-4337, Vol. 189, No. 11
0021-9193/07/$08.00+0 doi:10.1128/JB.01829-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.
,
Laetitia Fontaine,1
Jean-Luc Mainardi,2
Richard Daniel,3
Jeff Errington,3
Bernard Hallet,1 and
Pascal Hols1*
Unité de Génétique, Institut des Sciences de la Vie, Université catholique de Louvain, 1348 Louvain-la-Neuve, Belgium,1 INSERM, U655-LRMA, Université Paris 6, Université Paris-Descartes, Centre de Recherche Biomedicales des Cordeliers, Paris, F-75006, France,2 Institute for Cell and Molecular Biosciences, The Medical School, University of New Castle upon Tyne, New Castle upon Tyne NE2 4HH, United Kingdom3
Received 6 December 2006/ Accepted 19 March 2007
Lactobacillus plantarum produces peptidoglycan precursors ending in D-lactate instead of D-alanine, making the bacterium intrinsically resistant to vancomycin. The ligase Ddl of L. plantarum plays a central role in this specificity by synthesizing D-alanyl-D-lactate depsipeptides that are added to the precursor peptide chain by the enzyme MurF. Here we show that L. plantarum also encodes a D-Ala-D-Ala dipeptidase, Aad, which eliminates D-alanyl-D-alanine dipeptides that are produced by the Ddl ligase, thereby preventing their incorporation into the precursors. Although D-alanine-ended precursors can be incorporated into the cell wall, inactivation of Aad failed to suppress growth defects of L. plantarum mutants deficient in D-lactate-ended precursor synthesis.
Published ahead of print on 30 March 2007.
Supplemental material for this article may be found at http://jb.asm.org/.
Present address: Wageningen Centre for Food Sciences, NIZO Food Research, 6710 BA Ede, The Netherlands.
This article has been cited by other articles:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»