Elsevier

Gene

Volume 86, Issue 1, 31 January 1990, Pages 81-88
Gene

Modular organization of the lytic enzymes of Streptococcus pneumoniae and its bacteriophages

https://doi.org/10.1016/0378-1119(90)90116-9Get rights and content

Abstract

The nucleotide sequences of genes cpl7 and cpl9 of the Streptococcus pneumoniae bacteriophages Cp-7 and Cp-9, encoding the muramidases CPL-7 and CPL-9, respectively, have been determined. The N-terminal domains of CPL-7 and CPL-9 were virtually identical to that previously reported for the CPL-1 muramidase. The C-terminal domain of the CPL-7 muramidase, however, was different from those of the host amidase and the phage Cp-1 and Cp-9 lysozymes. Whereas all enzymes studied are characterized by repeated sequences at their C termini, the repeat-unit lengths are 20 amino acids (aa) in CPL-1, CPL-9 and in the host amidase, but 48 aa in CPL-7. Six repeated sequences represent the C-terminal domains of CPL-1, CPL-9 and the host amidase, and 2.8 perfect tandem repetitions that of CPL-7. The peculiar characteristics of the structure of CPL-7 muramidase correlate with its biochemical and biological properties. Whereas CPL-1, CPL-9 and the pneumococcal amidase strictly depend on the presence of choline-containing cell walls for activity, CPL-7 is able to degrade cell walls containing either choline or ethanolamine. These results support the previously postulated role for the C-terminal domain of these lytic enzymes in substrate recognition and provide further experimental evidence supporting the notion that the proteins have evolved by an exchange of modular units.

References (34)

  • E.M. Southern

    Detection of specific sequences among DNA fragments separated by electrophoresis

    J. Mol. Biol.

    (1975)
  • T.S. Balganesh et al.

    Construction and use of chimeric SPR-ø3T DNA methyltransferase in the definition of sequence recognizing enzyme domains

    EMBO J.

    (1987)
  • H.C. Birnboim et al.

    A rapid alkaline extraction procedure for screening recombinant plasmid DNA

    Nucleic Acids Res.

    (1979)
  • D. Botstein

    A theory of modular evolution for bacteriophages

    Ann. NY Acad. Sci.

    (1980)
  • H. Boyer et al.

    A complementation analysis of the restriction and modification of DNA in Escherichia coli

    J. Mol. Biol.

    (1969)
  • R.F. Doolittle

    Of URFs and ORFs

    (1986)
  • P. Garcia et al.

    Inhibition of lysis by antibody against phage-associated lysin and requirement of choline residues in the cell wall for progeny phage release in Streptococcus pneumoniae

    Curr. Microbiol.

    (1983)
  • Cited by (133)

    • Bacteriophages Infecting Lactic Acid Bacteria

      2017, Cheese: Chemistry, Physics and Microbiology: Fourth Edition
    • The Potential Use of Bacteriophage Therapy as a Treatment Option in a Post-Antibiotic Era

      2016, Antibiotic Resistance: Mechanisms and New Antimicrobial Approaches
    • Expression of Recombinant pET22b-LysK-Cysteine/Histidine-Dependent Amidohydrolase/Peptidase Bacteriophage Therapeutic Protein in Escherichia coli BL21 (DE3)

      2015, Osong Public Health and Research Perspectives
      Citation Excerpt :

      Unlike antibiotics, intact endolysins are large proteins that are capable of stimulating a humoral immune response, especially when they are used intravenously. Most endolysins have a modular organization with a conserved N-terminal catalytic domain and a more diverse C-terminal cell wall binding domain [37,38]. However, several S. aureus phages produce endolysins with two catalytic domains at their N terminus, such as those from phages K, f11, and fMR11.

    • Structure and Function of Choline-Binding Proteins

      2015, Streptococcus Pneumoniae: Molecular Mechanisms of Host-Pathogen Interactions
    View all citing articles on Scopus
    View full text