Function of T4D structural dihydrofolate reductase in bacteriophage infection.

Abstract

Various properties of the bacteriophage structural dihydrofolate reductase (DFR) have been examined to determine its function during phage infection. It has been found that a binding site for reduced nicotinamide adenine dinucleotide phosphate (NADPH), most likely on the DFR present in the phage tail plate, is required for phage viability. Attachment of adenosine diphosphoribose, an analogue of NADPH, to this site prevents phage adsorption and injection. This adenosine diphosphoribose inhibition can be competitively reversed by the addition of NADPH or oxidized nicotinamide adenine dinucleotide phosphate. It is suggested that, during phage infection, the host bacterial cell might leak compounds functionally similar to the pyridine nucleotides. These compounds have been shown to nonenzymatically change the conformation of the phage tail plate DFR which is apparently necessary for successful injection.

• Authors: C J Male, L M Kozloff
• Journal: Journal of virology (J Virol) Vol. 11 Issue 6 Pg. 840-7 (Jun 1973) ISSN: 0022-538X [Print] United States
• PMID: 4145894 (Publication Type: Journal Article)

Chemical References

• Adenine Nucleotides
• Pyrimidine Nucleotides
• NADP
• Tetrahydrofolate Dehydrogenase

Topics

• Adenine Nucleotides (pharmacology)
• Adsorption
• Binding Sites
• Cell Membrane Permeability
• Coliphages (drug effects, enzymology, growth & development)
• Drug Resistance, Microbial
• Escherichia coli
• Hot Temperature
• Hydrogen-Ion Concentration
• Mutation
• NADP (pharmacology)
• Pyrimidine Nucleotides (pharmacology)
• Tetrahydrofolate Dehydrogenase