Browse by author
Lookup NU author(s): Dr Richard Daniel,
Professor Jeff Errington FRSORCiD
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
Cell wall peptidoglycan assembly is a tightly regulated process requiring the combined action of multienzyme complexes. In this study we provide direct evidence showing that substrate transformations occurring at the different stages of this process play a crucial role in the spatial and temporal coordination of the cell wall synthesis machinery. Peptidoglycan substrate alteration was investigated in the Gram-positive bacterium Lactococcus lactis by substituting the peptidoglycan precursor biosynthesis genes of this bacterium for those of the vancomycin-resistant bacterium Lactobacillus plantarum. A set of L. lactis mutant strains in which the normal D-Ala-ended precursors were partially or totally replaced by D-Lac-ended precursors was generated. Incorporation of the altered precursor into the cell wall induced morphological changes arising from a defect in cell elongation and cell separation. Structural analysis of the muropeptides confirmed that the activity of multiple enzymes involved in peptidoglycan synthesis was altered. Optimization of this altered pathway was necessary to increase the level of vancomycin resistance conferred by the utilization of D-Lac-ended peptidoglycan precursors in the mutant strains. The implications of these findings on the control of bacterial cell morphogenesis and the mechanisms of vancomycin resistance are discussed.
Author(s): Deghorain M, Fontaine L, David B, Mainardi JL, Courtin P, Daniel R, Errington J, Sorokin A, Bolotin A, Chapot-Chartier MP, Hallet B, Hols P
Publication type: Article
Publication status: Published
Journal: Journal of Biological Chemistry
Print publication date: 01/07/2010
ISSN (print): 0021-9258
ISSN (electronic): 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology, Inc.
Altmetrics provided by Altmetric