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. 1991 Jan 15;273(Pt 2)(Pt 2):469-75.
doi: 10.1042/bj2730469.

DNA methylase from Pisum sativum

H M Yesufu  1 , A Hanley, A Rinaldi, R L Adams
Affiliations

DNA methylase from Pisum sativum

H M Yesufu et al. Biochem J. .

Abstract

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.

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