Inactivation of de novo DNA methyltransferase activity by high concentrations of double-stranded DNA
| Autor: | D. Drahovsky, Matilde Rispoli, Edward P. Whitehead, Stefan Grünwald, Franco Palitti, Roberto Strom, C. Salerno, Daniela Carotti |
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| Jazyk: | angličtina |
| Rok vydání: | 1987 |
| Předmět: |
DNA
Bacterial Methyltransferase Biophysics DNA Single-Stranded Eukaryotic DNA replication Biochemistry DNA methyltransferase Micrococcus chemistry.chemical_compound Polydeoxyribonucleotides Structural Biology Genetics DNA (Cytosine-5-)-Methyltransferases chemistry.chemical_classification Methionine biology DNA biology.organism_classification Molecular biology Enzyme assay Enzyme Activation Enzyme chemistry biology.protein De novo DNA methylation DNA (Cytosine-5-)-Methyltransferase DNA methyltransferase inactivation Micrococcus luteus |
| Popis: | The activity of eukaryotic DNA methyltransferase diminishes with time when the enzyme is incubated with high concentrations (200–300 μg/ml) of unmethylated double-stranded Micrococcus luteus DNA. Under similar conditions, single-stranded DNA induces only a limited decrease of enzyme activity. The inactivation process is apparently due to a slowly progressive interaction of the enzyme with double-stranded DNA that is independent of the presence of S- adenosyl- l -methionine . The inhibited enzyme cannot be reactivated either by high salt dissociation of the DNA-enzyme complex or by extensive digestion of the DNA. Among synthetic polydeoxyribonucleotides both poly(dG-dC) · poly(dG-dC) and poly(dA-dT) · poly(dA-dT), but not poly(dI-dC) · poly(dI-dC), cause inactivation of DNA methyltransferase. This inactivation process may be of interest in regulating the ‘de novo’ activity of the enzyme. |
| Databáze: | OpenAIRE |
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