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
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Research Support, Non-U.S. Gov't
MeSH terms
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Amidohydrolases / genetics
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Amidohydrolases / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacteriophages / chemistry*
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Bacteriophages / enzymology
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Bacteriophages / genetics*
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Base Sequence
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Electrophoresis, Polyacrylamide Gel
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Glycoside Hydrolases / genetics
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Glycoside Hydrolases / metabolism
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Lactococcus / chemistry*
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Lactococcus / enzymology
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Lactococcus / virology
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Molecular Sequence Data
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Plasmids
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Protein Structure, Tertiary
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / genetics
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Streptococcus pneumoniae / chemistry
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Streptococcus pneumoniae / enzymology
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Viral Structural Proteins / chemistry
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Viral Structural Proteins / genetics*
Substances
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Bacterial Proteins
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Recombinant Fusion Proteins
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S protein, bacteriophage Tuc2009
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Viral Structural Proteins
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Glycoside Hydrolases
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Amidohydrolases
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amidase