Abstract
Most point substitutions in the highly-conserved 885-GDTDS motif of the HSV-1 DNA polymerase inactivate polymerase elongation activity. However, in an assay system based on expression by in vitro transcription-translation, the mutant GDTDA (S889A) possessed wild-type elongation activity which was highly resistant to phosphonoacetic acid and acyclovir triphosphate, but retained sensitivity to aphidicolin.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Antiviral Agents / pharmacology*
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Base Sequence
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Cloning, Molecular
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Conserved Sequence*
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DNA, Viral
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DNA-Directed DNA Polymerase / genetics*
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DNA-Directed DNA Polymerase / metabolism
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Drug Resistance, Microbial / genetics
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Electrophoresis, Polyacrylamide Gel
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Exodeoxyribonucleases / genetics*
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Exodeoxyribonucleases / metabolism
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Point Mutation
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Viral Proteins*
Substances
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Antiviral Agents
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DNA, Viral
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Viral Proteins
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DNA-Directed DNA Polymerase
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Exodeoxyribonucleases
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DNA polymerase, Simplexvirus