Purification and characterization of the lytic activity induced by the prolate-headed bacteriophage P001 in Lactococcus lactis.
The lytic activity induced by the lactococcal bacteriophage P001 was isolated from phage lysates of Lactococcus lactis by a four-step purification procedure. Two proteins lytic for L. lactis were identified with molecular weights of 28 kDA and 8 kDa, respectively. The N-terminal amino acid sequences of the two proteins were determined and degenerated oligonucleotide probes corresponding to these sequences were synthesized. DNA hybridization experiments with phage P001-DNA and lactococcal DNA revealed that both proteins were apparently encoded by a single lysin gene located on the phage P001 genome. This was confirmed by alignment of the determined N-terminal amino acid sequences with nucleotide sequences which were deduced from cloned Lactococcus bacteriophage lysin genes.
Hertwig
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S
Bockelmann
W
W
Teuber
M
M
D001435:Bacteriophages / Q000201:enzymology* / Q000235:genetics; D015153:Blotting, Western; D004591:Electrophoresis, Polyacrylamide Gel; D005814:Genes, Viral; D016679:Genome, Viral; D013294:Lactococcus lactis / Q000821:virology*; D009088:Mucoproteins / Q000235:genetics*; D015345:Oligonucleotide Probes; D014764:Viral Proteins / Q000235:genetics*; D015678:Viral Structural Proteins / Q000235:genetics
D009088:Mucoproteins; D015345:Oligonucleotide Probes; D014764:Viral Proteins; D015678:Viral Structural Proteins; C010393:lysin, gastropoda