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Permanent link (DOI): https://doi.org/10.7939/R3R49GM29

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Analysis of inhibitors of bacteriophage T4 DNA polymerase Open Access

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Author or creator
Khan, N.N.
Reha-Krantz, L.J.
Wright, G.E.
Additional contributors
Subject/Keyword
mechanism
aphidicolin
binding
alpha
5'-Triphosphate
Herpes-Simplex Virus
derivatives
delta
polymerization
replication
Type of item
Journal Article (Published)
Language
English
Place
Time
Description
Bacteriophage T4 DNA polymerase was Inhibited by butylphenyl nucleotldes, aphldlcolin and pyrophosphate analogs, but with lower sensitivities than other members of the B family DNA polymerases. The nucleotides N2-{p-n-butylphenyl)dGTP (BuPdGTP) and 2-{p-n-butylanilino)dATP (BuAdATP) inhibited T4 DNA polymerase with competitive K< values of 0.82 and 0.54 /iM with respect to dGTP and dATP, respectively. The same compounds were more potent Inhibitors In truncated assays lacking the competitor dNTP, displaying apparent K< values of 0.001 and 0.0016 /xM, respectively. BuPdGTP was a substrate for T4 DNA polymerase, and the resulting 3-BuPdGprimer: template was bound strongly by the enzyme. Each of the non-substrate derivatives, BuPdGDP and BuPdGMPCH2PP, inhibited T4 DNA polymerase with similar potencies in both the truncated and variable competitor assays. These results Indicate that BuPdGTP inhibits T4 DNA polymerase by distinct mechanisms depending upon the assay conditions. Reversible competitive inhibition predominates in the presence of dGTP, and incorporation in the absence of dGTP leads to potent Inhibition by the modified primer template. The Implications of these findings for the use of these Inhibitors In the study of B family DNA polymerases Is discussed.
Date created
1994
DOI
doi:10.7939/R3R49GM29
License information
Rights
© 1994 Oxford University Press
Citation for previous publication
N N Khan, L J Reha-Krantz, and G E Wright (1994). Analysis of inhibitors of bacteriophage T4 DNA polymerase. Nucleic Acids Res. 22(2): 232–237. DOI: 10.1093/nar/22.2.232
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