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Functional and Morphological Adaptation to Peptidoglycan Precursor Alteration in Lactococcus lactis

Lookup NU author(s): Dr Richard Daniel, Professor Jeff Errington

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Abstract

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.


Publication metadata

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

Year: 2010

Volume: 285

Issue: 31

Pages: 24003-24013

Print publication date: 01/07/2010

ISSN (print): 0021-9258

ISSN (electronic): 1083-351X

Publisher: American Society for Biochemistry and Molecular Biology, Inc.

URL: http://dx.doi.org/10.1074/jbc.M110.143636

DOI: 10.1074/jbc.M110.143636


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