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Bacteriophage tail components. I. Pteroyl polyglutamates in T-even bacteriophages
Journal of Virology
|June 1, 1970
Summary
Escherichia coli T-even bacteriophages contain a unique dihydropteroyl polyglutamate compound. This phage-specific molecule is synthesized only after infection and is likely located at the bacteriophage tail structure.
Area of Science:
- Microbiology
- Molecular Biology
- Virology
Background:
- Pteroylpolyglutamates are essential cofactors in various metabolic pathways.
- The presence and role of pteroylpolyglutamates in bacteriophages have not been extensively studied.
Purpose of the Study:
- To characterize the pteroylpolyglutamate found in Escherichia coli T-even bacteriophages.
- To determine the origin, synthesis, and location of this phage-associated compound.
Main Methods:
- Chemical and physical property analysis of the phage compound.
- Analysis of E. coli extracts from infected and uninfected cells.
- Investigation of synthesis sensitivity to chloramphenicol.
- Examination of isolated phage particles, including ghost and tail substructures.
Main Results:
- A dihydropteroyl penta- or hexaglutamate was identified as a constituent of all T-even bacteriophages.
- The phage-specific pteroylpolyglutamate was detected only in infected E. coli cells and its synthesis was induced by phage infection.
- Each phage particle contains 2-6 pteroyl derivatives, primarily bound at the tail plate-tail tube junction.
Conclusions:
- Escherichia coli T-even bacteriophages encode or induce the synthesis of a specific dihydropteroyl polyglutamate.
- This compound is an integral part of the phage particle, likely playing a role in infection, and is localized to the tail structure.