Function of T4D Structural Dihydrofolate Reductase in Bacteriophage Infection
AUTOR(ES)
Male, Carolyn J.
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=355190Documentos Relacionados
- Bacteriophage Tail Components: II. Dihydrofolate Reductase in T4D Bacteriophage
- Inactivation of T4D Bacteriophage by Antiserum Against Bacteriophage Dihydrofolate Reductase
- Dominance in Bacteriophage T4d
- Polynucleotide Ligase in Bacteriophage T4d Recombination
- Bacteriophage T4 Virion Dihydrofolate Reductase: Approaches to Quantitation and Assessment of Function
