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Incorporation of d-alanine into lipoteichoic acid and wall teichoic-acid in bacillus-subtilis - identification of genes and regulation

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Overview

authors

  • Perego, Marta
  • Glaser, P.
  • Minutello, A.
  • Strauch, M. A.
  • Leopold, K.
  • Fischer, W.

publication date

  • 1995

journal

  • Journal of Biological Chemistry  Journal

abstract

  • 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 sigma D-dependent promoter and follows the pattern of transcription of genes belonging to the sigma D 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.

subject areas

  • Alanine
  • Amino Acid Sequence
  • Bacillus subtilis
  • Base Sequence
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Lipopolysaccharides
  • Molecular Sequence Data
  • Operon
  • Teichoic Acids
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

PubMed ID

  • 7797557
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Additional Document Info

start page

  • 15598

end page

  • 15606

volume

  • 270

issue

  • 26

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