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Bacillus subtilis 168 gene lytF encodes a -D-glutamate-meso-diaminopimelate muropeptidase expressed by the alternative vegetative sigma factor, ^D

Institut de génétique et de biologie microbiennes, Rue César-Roux 19, CH-1005 Lausanne, Switzerland

Author for correspondence: Dimitri Karamata. Tel: +41 21 3206075. Fax: +41 21 3206078. e-mail: dimitri.karamata@igbm.unil.ch

ABSTRACT

Summary: A -D-glutamate-meso-diaminopimelate muropeptidase was detected in the vegetative growth phase of Bacillus subtilis 168. It is encoded by the monocistronic lytF operon expressed by the alternative vegetative sigma factor, ^D. Sequence analysis of LytF revealed two domains, an organization common to exoproteins of B. subtilis as well as to those from other organisms. The N-terminal domain contains a fivefold-repeated motif attributed to cell wall binding, whilst the C-terminal domain is probably endowed with the catalytic activity. Overrexpression of LytF allowed its purification and biochemical characterization. Inactivation of lytF led to the loss of the cell-wall-bound protein 49' (CWBP49') and of the corresponding lytic activity as revealed by renaturation gel assay. Native cell walls prepared from the multiple lytC lytD lytE lytF-deficient mutant did not exhibit any autolysis, whereas walls prepared from a strain endowed with LytF but not with the other three enzymes underwent a slight lysis. Analysis of degradation products of cell wall devoid of teichoic-acid-bound O-esterified D-alanine unambiguously confirmed that LytF cuts the -D-glutamate-meso-diaminopimelate bond.

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