DNA binding and methyl transfer catalysed by mouse DNA methyltransferase

Reale, Anna; Lindsay, H.; Saluz, H. P.; Pradhan, S.; Adams, R. L. P.; Jost, J. P.; Strom, Roberto

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-adenosylmethionine 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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Titolo:	DNA binding and methyl transfer catalysed by mouse DNA methyltransferase
Autori:	REALE, Anna H. Lindsay H. P. Saluz S. Pradhan R. L. P. Adams J. P. Jost STROM, Roberto mostra contributor esterni nascondi contributor esterni
Data di pubblicazione:	1995
Rivista:	BIOCHEMICAL JOURNAL
Handle:	http://hdl.handle.net/11573/388247
Appartiene alla tipologia:	01a Articolo in rivista

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