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Mechanistic details of the DNA recognition by the Dnmt1 DNA methyltransferase


, : Mechanistic details of the DNA recognition by the Dnmt1 DNA methyltransferase. Febs Letters 586(13): 1821-1823

A recently solved Dnmt1-DNA crystal structure revealed several enzyme-DNA contacts and large structural rearrangements of the DNA at the target site, including the flipping of the non-target strand base of the base pair flanking the CpG site and formation of a non-canonical base pair between the non-target strand Gua and the flanking base pair. Here, we show that the contacts of the enzyme to the target base and the Gua:5mC base pair that are observed in the structure are very important for catalytic activity. The contacts to the non target strand Gua are not important since its exchange by Ade stimulated activity. Except target base flipping, we could not find evidence that the DNA rearrangements have a functional role. Recently the Dnmt1-DNA crystal structure was solved. Contacts of the enzyme to the target base and the Gua:5mC base pair are very important for catalytic activity. Contacts to the non target strand Gua are not important since its exchange by Ade stimulated activity. DNA rearrangements, except the flipping of the target base, do not appear to have a functional role.

US$19.90

PMID: 22641038

DOI: 10.1016/j.febslet.2012.05.026


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