| Literature DB >> 1991042 |
H M Yesufu1, A Hanley, A Rinaldi, R L Adams.
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.Entities:
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Year: 1991 PMID: 1991042 PMCID: PMC1149868 DOI: 10.1042/bj2730469
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857