This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Debabov, D. V.
Right arrow Articles by Neuhaus, F. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Debabov, D. V.
Right arrow Articles by Neuhaus, F. C.

 Previous Article  |  Next Article 

J. Bacteriol., 07 1996, 3869-3876, Vol 178, No. 13
Copyright © 1996, American Society for Microbiology

The D-Alanyl carrier protein in Lactobacillus casei: cloning, sequencing, and expression of dltC

DV Debabov, MP Heaton, Q Zhang, KD Stewart, RH Lambalot and FC Neuhaus
Department of Biochemistry, Molecular and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA.

The incorporation of D-alanine into membrane-associated D-alanyl- lipoteichoic acid in Lactobacillus casei requires the 56-kDa D-alanine- D-alanyl carrier protein ligase (Dcl) and the 8.9-kDa D-alanyl carrier protein (Dcp). To identify and isolate the gene encoding Dcp, we have cloned and sequenced a 4.3-kb chromosomal fragment that contains dcl (dltA). In addition to this gene, the fragment contains three other genes, dltB, d1tC, and a partial dltD gene. dltC (246 nucleotides) was subcloned from this region and expressed in Escherichia coli. The product was identified as apo-Dcp lacking the N-terminal methionine (8,787.9 Da). The in vitro conversion of the recombinant apo-Dcp to holo-Dcp by recombinant E. coli holo-ACP synthase provided Dcp which accepts activated D-alanine in the reaction catalyzed by Bcl. The recombinant D-alanyl-Dcp was functionally identical to native D-alanyl- Dcp in the incorporation of D-alanine into lipoteichoic acid. L. casei Dcp is 46% identical to the putative product of dltC in the Bacillus subtilis dlt operon (M. Perego, P. Glaser, A. Minutello, M. A. Strauch, K. Leopold, and W. Fischer, J. Biol. Chem. 270:15598-15606, 1995), and therefore, this gene also encodes Dcp. Comparisons of the primary sequences and predicted secondary structures of the L. casei and B. subtilis Dcps with that of the E. coli acyl carrier protein (ACP) were undertaken together with homology modeling to identify the functional determinants of the donor and acceptor specificities of Dcp. In the region of the phospho-pantetheine attachment site, significant similarity between Dcps and ACPs was observed. This similarity may account for the relaxed acceptor specificity of the Dcps and ACPs in the ligation Of D-alanine catalyzed by Dcl. In contrast, two Dcp consensus sequences, KXXVLDXLA and DXVKXNXD, share little identity with the rest of the ACP family and, thus, may determine the donor specificity of D-alanyl-Dcp in the D-alanylation of membrane-associated D-alanyl-lipoteichoic acid.


This article has been cited by other articles:

  • Abi Khattar, Z., Rejasse, A., Destoumieux-Garzon, D., Escoubas, J. M., Sanchis, V., Lereclus, D., Givaudan, A., Kallassy, M., Nielsen-Leroux, C., Gaudriault, S. (2009). The dlt Operon of Bacillus cereus Is Required for Resistance to Cationic Antimicrobial Peptides and for Virulence in Insects. J. Bacteriol. 191: 7063-7073 [Abstract] [Full Text]  
  • Velez, M. P., Verhoeven, T. L. A., Draing, C., Von Aulock, S., Pfitzenmaier, M., Geyer, A., Lambrichts, I., Grangette, C., Pot, B., Vanderleyden, J., De Keersmaecker, S. C. J. (2007). Functional Analysis of D-Alanylation of Lipoteichoic Acid in the Probiotic Strain Lactobacillus rhamnosus GG. Appl. Environ. Microbiol. 73: 3595-3604 [Abstract] [Full Text]  
  • Kovacs, M., Halfmann, A., Fedtke, I., Heintz, M., Peschel, A., Vollmer, W., Hakenbeck, R., Bruckner, R. (2006). A Functional dlt Operon, Encoding Proteins Required for Incorporation of D-Alanine in Teichoic Acids in Gram-Positive Bacteria, Confers Resistance to Cationic Antimicrobial Peptides in Streptococcus pneumoniae.. J. Bacteriol. 188: 5797-5805 [Abstract] [Full Text]  
  • Palumbo, E., Deghorain, M., Cocconcelli, P. S., Kleerebezem, M., Geyer, A., Hartung, T., Morath, S., Hols, P. (2006). D-Alanyl Ester Depletion of Teichoic Acids in Lactobacillus plantarum Results in a Major Modification of Lipoteichoic Acid Composition and Cell Wall Perforations at the Septum Mediated by the Acm2 Autolysin.. J. Bacteriol. 188: 3709-3715 [Abstract] [Full Text]  
  • Leonardi, R., Chohnan, S., Zhang, Y.-M., Virga, K. G., Lee, R. E., Rock, C. O., Jackowski, S. (2005). A Pantothenate Kinase from Staphylococcus aureus Refractory to Feedback Regulation by Coenzyme A. J. Biol. Chem. 280: 3314-3322 [Abstract] [Full Text]  
  • Franklin, M. J., Douthit, S. A., McClure, M. A. (2004). Evidence that the algI/algJ Gene Cassette, Required for O Acetylation of Pseudomonas aeruginosa Alginate, Evolved by Lateral Gene Transfer. J. Bacteriol. 186: 4759-4773 [Abstract] [Full Text]  
  • Neuhaus, F. C., Baddiley, J. (2003). A Continuum of Anionic Charge: Structures and Functions of D-Alanyl-Teichoic Acids in Gram-Positive Bacteria. Microbiol. Mol. Biol. Rev. 67: 686-723 [Abstract] [Full Text]  
  • Mofid, M. R., Finking, R., Marahiel, M. A. (2002). Recognition of Hybrid Peptidyl Carrier Proteins/Acyl Carrier Proteins in Nonribosomal Peptide Synthetase Modules by the 4'-Phophopantetheinyl Transferases AcpS and Sfp. J. Biol. Chem. 277: 17023-17031 [Abstract] [Full Text]  
  • Poyart, C., Lamy, M. C., Boumaila, C., Fiedler, F., Trieu-Cuot, P. (2001). Regulation of D-Alanyl-Lipoteichoic Acid Biosynthesis in Streptococcus agalactiae Involves a Novel Two-Component Regulatory System. J. Bacteriol. 183: 6324-6334 [Abstract] [Full Text]  
  • Kiriukhin, M. Y., Neuhaus, F. C. (2001). D-Alanylation of Lipoteichoic Acid: Role of the D-Alanyl Carrier Protein in Acylation. J. Bacteriol. 183: 2051-2058 [Abstract] [Full Text]  
  • Boyd, D. A., Cvitkovitch, D. G., Bleiweis, A. S., Kiriukhin, M. Y., Debabov, D. V., Neuhaus, F. C., Hamilton, I. R. (2000). Defects in D-Alanyl-Lipoteichoic Acid Synthesis in Streptococcus mutans Results in Acid Sensitivity. J. Bacteriol. 182: 6055-6065 [Abstract] [Full Text]  
  • Debabov, D. V., Kiriukhin, M. Y., Neuhaus, F. C. (2000). Biosynthesis of Lipoteichoic Acid in Lactobacillus rhamnosus: Role of DltD in D-Alanylation. J. Bacteriol. 182: 2855-2864 [Abstract] [Full Text]  
  • Flugel, R. S., Hwangbo, Y., Lambalot, R. H., Cronan, J. E. Jr., Walsh, C. T. (2000). Holo-(Acyl Carrier Protein) Synthase and Phosphopantetheinyl Transfer in Escherichia coli. J. Biol. Chem. 275: 959-968 [Abstract] [Full Text]  
  • Clemans, D. L., Kolenbrander, P. E., Debabov, D. V., Zhang, Q., Lunsford, R. D., Sakone, H., Whittaker, C. J., Heaton, M. P., Neuhaus, F. C. (1999). Insertional Inactivation of Genes Responsible for the D-Alanylation of Lipoteichoic Acid in Streptococcus gordonii DL1 (Challis) Affects Intrageneric Coaggregations. Infect. Immun. 67: 2464-2474 [Abstract] [Full Text]  
  • Pfennig, F., Schauwecker, F., Keller, U. (1999). Molecular Characterization of the Genes of Actinomycin Synthetase I and of a 4-Methyl-3-hydroxyanthranilic Acid Carrier Protein Involved in the Assembly of the Acylpeptide Chain of Actinomycin in Streptomyces. J. Biol. Chem. 274: 12508-12516 [Abstract] [Full Text]  
  • Spatafora, G. A., Sheets, M., June, R., Luyimbazi, D., Howard, K., Hulbert, R., Barnard, D., el Janne, M., Hudson, M. C. (1999). Regulated Expression of the Streptococcus mutans dlt Genes Correlates with Intracellular Polysaccharide Accumulation. J. Bacteriol. 181: 2363-2372 [Abstract] [Full Text]  
  • Navarre, W. W., Schneewind, O. (1999). Surface Proteins of Gram-Positive Bacteria and Mechanisms of Their Targeting to the Cell Wall Envelope. Microbiol. Mol. Biol. Rev. 63: 174-229 [Abstract] [Full Text]  
  • Mootz, H. D., Finking, R., Marahiel, M. A. (2001). 4'-Phosphopantetheine Transfer in Primary and Secondary Metabolism of Bacillus subtilis. J. Biol. Chem. 276: 37289-37298 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»