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. 1995 Dec 15;312 ( Pt 3)(Pt 3):855-61.
doi: 10.1042/bj3120855.

DNA binding and methyl transfer catalysed by mouse DNA methyltransferase

A Reale  1 , H Lindsay, H P Saluz, S Pradhan, R L Adams, J P Jost, R Strom
Affiliations

DNA binding and methyl transfer catalysed by mouse DNA methyltransferase

A Reale et al. Biochem J. .

Abstract

By using a purified fraction of mouse DNA methyltransferase we have shown, by gel-retardation analysis, that the enzyme forms a low-affinity complex preferentially with hemimethylated DNA; the complexes formed with unmethylated or with fully methylated DNA are of even lower affinity, and only very weak interaction occurs with DNA lacking CG dinucleotides. Interaction is inhibited by N-ethylmaleimide. Methyl transfer from S-adenosyl-methionine is associated with the release of the fully methylated product from the complex. Complexes formed with the intact enzyme are extremely large, but limited trypsin treatment allows a major complex to enter the gel. DNA binding is not inhibited by this limited proteolysis of the native enzyme.

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