| Autor: |
Yesufu HM; Department of Biochemistry, University of Glasgow, U.K., Hanley A, Rinaldi A, Adams RL |
| Jazyk: |
angličtina |
| Zdroj: |
The Biochemical journal [Biochem J] 1991 Jan 15; Vol. 273(Pt 2), pp. 469-75. |
| DOI: |
10.1042/bj2730469 |
| Abstrakt: |
DNA methylase activity was detected in nuclei from pea shoots. The enzyme can only be extracted by low-salt treatment if the nuclei are pretreated with micrococcal nuclease. Only a single enzyme was detected, and it was purified to a specific activity of 1620 units/mg of protein. It has an Mr of 160,000 on gel filtration and SDS/PAGE. Pea DNA methylase methylates cytosine in all four dinucleotides, and this is interpreted to show that it acts on CNG trinucleotides. Although it shows a strong preference for hemi-methylated double-stranded DNA, it is also capable of methylation de novo. Homologous DNA is the best natural substrate. In vitro the enzyme interacts with DNA to form a salt-resistant complex with DNA that is stable for at least 4 h. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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