Bacteriophage Tail Components
@article{Kozloff1970BacteriophageTC,
title={Bacteriophage Tail Components},
author={Lloyd M. Kozloff and Murl Lute and L K Crosby and Na Rao and V. A. Chapman and S Delong},
journal={Journal of Virology},
year={1970},
volume={5},
pages={726 - 739}
}A pteroylpolyglutamate has been found to be a constituent of all Escherichia coli T-even bacteriophages and has been characterized with regard to its oxidation state, molecular weight, origin, and location on the phage particle. The phage compound has been shown to be a dihydropteroyl penta- or hexaglutamate on the basis of its chemical and physical properties. Analyses of extracts of uninfected and T2L-infected E. coli have indicated that the phage dihydropteroyl polyglutamate was present only…
41 Citations
Folate polyglutamates in T4D bacteriophage and T4D-infected Escherichia coli.
- BiologyBiochimica et biophysica acta
- 1978
Bacteriophage T4D Receptor and the Escherichia coli Cell Wall Structure: Binding of Endotoxin-Like Particles to the Cell Wall
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A variety of degradative treatments have been used to investigate the nature of the structure and components of the cell walls of Escherichia coli B. The binding and localization of the…
Identification of T4 gene 25 product, a component of the tail baseplate, as a 15K lysozyme
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It has been found that the 15K lysozyme is not present in lysates of bacteria infected with T4 gene 25 amber mutants, and observations indicate that the15K ly sozyme is the gene 25 product.
Bacteriophage TailComponents IV.Pteroyl Polyglutamate Synthesis inT4D-Infected Escherichia coli B
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- 1973
It is found that, although themajorfolate compound inuninfected bacteria ispteroyl triglutamate, E.coli B cells also contain folate compounds having as many as sixglutamate residues, which ischloramphenicol sensitive andappearstobeduetoalate phage geneproduct.
DISCUSSION PAPER: BACTERIOPHAGE‐INDUCED DIHYDROFOLATE REDUCTASE
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- 1971
This work has purified dihydrofolate reductase from T4 phage-infected cells and found that the pure enzyme contains but one polypeptide subunit, which indicates that the system is amenable to genetic manipulation, allowing US, for example, to prepare genetically modified, catalytically inactive proteins.
Bacteriophage Tail Components
- BiologyJournal of virology
- 1970
The assembly of T4D tail plates occurring during in vitro complementation reactions was found to be stimulated by pteroyl hexaglutamate. Neither the pteroyl pentaglutamate nor the pteroyl…
An immunoblot assay reveals that bacteriophage T4 thymidylate synthase and dihydrofolate reductase are not virion proteins
- BiologyJournal of virology
- 1995
A quantitative immunoblot assay shows that both phage T4 enzymes thymidylate synthase and dihydrofolate reductase are present only as minor contaminants and as such cannot be bona fide structural proteins.
Bacteriophage-coded thymidylate synthetase. Evidence that the T4 enzyme is a capsid protein.
- Biology, ChemistryArchives of biochemistry and biophysics
- 1973
Bacteriophage T4 tail assembly: four steps in core formation.
- BiologyJournal of molecular biology
- 1971
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