TY  - JOUR
  - Kenny, JG,McGrath, S,Fitzgerald, GF,van Sinderen, D
  - 2004
  - April
  - Journal of Bacteriology
  - Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity
  - Validated
  - ()
  - LACTOCOCCUS-LACTIS STREPTOCOCCUS-THERMOPHILUS ESCHERICHIA-COLI LYTIC ENZYME GLYCYLGLYCINE ENDOPEPTIDASE MOLECULAR CHARACTERIZATION STRUCTURAL PROTEINS MODULAR EVOLUTION CLONING VECTORS VIRAL MEMBRANE
  - 186
  - 3480
  - 3491
  - Tuc2009 is a P335-type member of the tailed-phage supergroup Siphoviridae and was originally identified as a resident prophage of the gram-positive bacterium Lactococcus lactis UC509. A Tuc2009 gene designated tal(2009) which is located within the morphogenic module was shown to specify a lytic activity within the 3' portion of its coding region. Comparative sequence analysis indicated that the cell wall-degrading part of Tal(2009) is a member of the M37 protein family and that Tal(2009) lacks a cell-binding domain, a finding supported by binding studies. Tal(2009) appears to undergo self-mediated posttranslational processing in both L. lactis and Escherichia coli. Antibodies directed against a purified C-terminal portion of Tal(2009) were used for immunoelectron microscopy, which showed that Tal(2009) is located at the tail tip of Tuc2009. Antibody neutralization studies demonstrated that Tal(2009)-directed antibodies inhibited the ability of phage to mediate host lysis by more than 100-fold. These data indicate that tal(2009) encodes a tail-associated lysin involved in localized cell wall degradation, thus allowing the Tuc2009 DNA injection machinery access to the membrane of its bacterial host.
  - DOI 10.1128/JB.186.11.3480.3491.2004
DA  - 2004/04
ER  - 

@article{V43337599,
   = {Kenny,  JG and McGrath,  S and Fitzgerald,  GF and van Sinderen,  D },
   = {2004},
   = {April},
   = {Journal of Bacteriology},
   = {Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity},
   = {Validated},
   = {()},
   = {LACTOCOCCUS-LACTIS STREPTOCOCCUS-THERMOPHILUS ESCHERICHIA-COLI LYTIC ENZYME GLYCYLGLYCINE ENDOPEPTIDASE MOLECULAR CHARACTERIZATION STRUCTURAL PROTEINS MODULAR EVOLUTION CLONING VECTORS VIRAL MEMBRANE},
   = {186},
  pages = {3480--3491},
   = {{Tuc2009 is a P335-type member of the tailed-phage supergroup Siphoviridae and was originally identified as a resident prophage of the gram-positive bacterium Lactococcus lactis UC509. A Tuc2009 gene designated tal(2009) which is located within the morphogenic module was shown to specify a lytic activity within the 3' portion of its coding region. Comparative sequence analysis indicated that the cell wall-degrading part of Tal(2009) is a member of the M37 protein family and that Tal(2009) lacks a cell-binding domain, a finding supported by binding studies. Tal(2009) appears to undergo self-mediated posttranslational processing in both L. lactis and Escherichia coli. Antibodies directed against a purified C-terminal portion of Tal(2009) were used for immunoelectron microscopy, which showed that Tal(2009) is located at the tail tip of Tuc2009. Antibody neutralization studies demonstrated that Tal(2009)-directed antibodies inhibited the ability of phage to mediate host lysis by more than 100-fold. These data indicate that tal(2009) encodes a tail-associated lysin involved in localized cell wall degradation, thus allowing the Tuc2009 DNA injection machinery access to the membrane of its bacterial host.}},
   = {DOI 10.1128/JB.186.11.3480.3491.2004},
  source = {IRIS}
}