par Deghorain, Marie ;Goffin, Philippe;Fontaine, Laetitia;Mainardi, Jean-Luc;Daniel, Richard;Errington, Jeff;Hallet, Bernard;Hols, Pascal
Référence Journal of bacteriology, 189, 11, page (4332-4337)
Publication Publié, 2007-06
Référence Journal of bacteriology, 189, 11, page (4332-4337)
Publication Publié, 2007-06
Article révisé par les pairs
Résumé : | 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. |