IRIS publication 43337599
Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity
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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 -
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@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} }
Data as stored in IRIS
AUTHORS | Kenny, JG,McGrath, S,Fitzgerald, GF,van Sinderen, D | ||
YEAR | 2004 | ||
MONTH | April | ||
JOURNAL_CODE | Journal of Bacteriology | ||
TITLE | Bacteriophage Tuc2009 encodes a tail-associated cell wall-degrading activity | ||
STATUS | Validated | ||
TIMES_CITED | () | ||
SEARCH_KEYWORD | LACTOCOCCUS-LACTIS STREPTOCOCCUS-THERMOPHILUS ESCHERICHIA-COLI LYTIC ENZYME GLYCYLGLYCINE ENDOPEPTIDASE MOLECULAR CHARACTERIZATION STRUCTURAL PROTEINS MODULAR EVOLUTION CLONING VECTORS VIRAL MEMBRANE | ||
VOLUME | 186 | ||
ISSUE | |||
START_PAGE | 3480 | ||
END_PAGE | 3491 | ||
ABSTRACT | 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. | ||
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DOI_LINK | DOI 10.1128/JB.186.11.3480.3491.2004 | ||
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