Bacteriophage Tail Components

  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},
  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… 

Bacteriophage T4D Receptor and the Escherichia coli Cell Wall Structure: Binding of Endotoxin-Like Particles to the Cell Wall

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

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

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.


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

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

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 T4 tail assembly: four steps in core formation.

  • J. King
  • Biology
    Journal of molecular biology
  • 1971



Folic acid, a structural component of T4 bacteriophage.

Morphogenesis of bacteriophage T4 in extracts of mutant-infected cells.

  • R. EdgarW. Wood
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1966
In the experiments reported below, conditional lethal mutants of strain T4D have been exploited to develop an in vitro system in which several of the steps in phage morphogenesis can be demonstrated.

Disruption of T-even Bacteriophages by Dimethyl Sulfoxide

Examination of the isolated free heads of T-even bacteriophage indicated that a distinct neck substructure was attached to one apex of the head, and it was concluded that this was a distinct substructure and not an extension of the tail tube.

Some steps in the assembly of bacteriophage T4.

Critical Arginine Residue for Maintaining the Bacteriophage Tail Structure

The addition of 0.2 m l-arginine to various T-even bacteriophage preparations inactivated the virus preparations irreversibly. The virus particles were even more sensitive to added d-arginine and


An assay based on the lytic action toward host cells has been developed which permits a rapid evaluation of the number of ghosts with a reliability of ±15 per cent and the antigenic and certain physicochemical properties of the ghost have been determined.