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Volume 270,
Number 26,
Issue of June 30, pp. 15598-15606, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Incorporation
of D-Alanine into Lipoteichoic Acid and Wall Teichoic Acid in Bacillus subtilis IDENTIFICATION OF GENES AND REGULATION
Marta
Perego
,
Philippe
Glaser
,
Antonia
Minutello
,
Mark
A.
Strauch
,
Klaus
Leopold
,
Werner
Fischer
The Bacillus subtilis dlt operon (D-alanyl-lipoteichoic acid) is responsible for D-alanine esterification of both lipoteichoic acid (LTA) and
wall teichoic acid (WTA). The dlt operon contains five genes, dltA-dltE. Insertional inactivation of dltA-dltD results in complete absence of D-alanine from both LTA and WTA. Based on protein sequence
similarity with the Lactobacillus casei dlt gene products
(Heaton, M. P., and Neuhaus, F. C.(1992) J.Bacteriol. 174, 4707-4717), we propose that dltA encodes the D-alanine-D-alanyl carrier
protein ligase (Dcl) and dltC the D-alanyl carrier
protein (Dcp). We further hypothesize that the products of dltB and dltD are concerned with the transport of
activated D-alanine through the membrane and the final
incorporation of D-alanine into LTA. The hydropathy profiles
of the dltB and dltD gene products suggest a
transmembrane location for the former and an amino-terminal signal
peptide for the latter. The incorporation of D-alanine into
LTA and WTA did not separate in any of the mutants studied which
indicates that either one and the same enzyme is responsible for D-alanine incorporation into both polymers or a separate
enzyme, encoded outside the dlt operon, transfers the D-alanyl residues from LTA to WTA (Haas, R., Koch, H.-U., and
Fischer, W.(1984) FEMS Microbiol. Lett. 21, 27-31).
Inactivation of dltE has no effect on D-alanine ester
content of both LTA and WTA, and at present we cannot propose any
function for its gene product. Transcription analysis shows that the dlt operon is transcribed from a  -dependent
promoter and follows the pattern of transcription of genes belonging to
the  regulon. However, the turn off of transcription
observed before sporulation starts seems to be dependent on the Spo0A
and AbrB sporulation proteins and results in a D-alanine-free
purely anionic LTA in the spore membrane. The dlt operon is
dispensable for cell growth; its inactivation does not affect cell
growth or morphology as described for L.casei.

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Copyright © 1995 by the American Society for Biochemistry and Molecular Biology.
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