Analysis of the Catalytic Domain of the Lysin of the Lactococcal Bacteriophage Tuc2009 by Chimeric Gene Assembling

FEMS Microbiol Lett. 1996 Jun 15;140(1):23-8. doi: 10.1111/j.1574-6968.1996.tb08309.x.

Abstract

An active chimeric cell wall lytic enzyme (Tsl) has been constructed by fusing the region coding for the N-terminal half of the lactococcal phage Tuc2009 lysin and the region coding for the C-terminal domain of the major pneumococcal autolysin. The chimeric enzyme exhibited a glycosidase activity capable of hydrolysing choline-containing pneumococcal cell walls. This experimental approach demonstrated that the Tuc2009 lysin possesses a modular structure and further supports the hypothesis that many cell wall lytic enzymes have evolved by the fusion of preexisting catalytic and peptidoglycan-binding domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacteriophages / chemistry*
  • Bacteriophages / enzymology
  • Bacteriophages / genetics*
  • Base Sequence
  • Electrophoresis, Polyacrylamide Gel
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism
  • Lactococcus / chemistry*
  • Lactococcus / enzymology
  • Lactococcus / virology
  • Molecular Sequence Data
  • Plasmids
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Streptococcus pneumoniae / chemistry
  • Streptococcus pneumoniae / enzymology
  • Viral Structural Proteins / chemistry
  • Viral Structural Proteins / genetics*

Substances

  • Bacterial Proteins
  • Recombinant Fusion Proteins
  • S protein, bacteriophage Tuc2009
  • Viral Structural Proteins
  • Glycoside Hydrolases
  • Amidohydrolases
  • amidase