Mechanistic details of the DNA recognition by the Dnmt1 DNA methyltransferase

FEBS Lett. 2012 Jun 21;586(13):1821-3. doi: 10.1016/j.febslet.2012.05.026. Epub 2012 May 26.

Abstract

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.

MeSH terms

  • Base Pairing
  • Base Sequence
  • Binding Sites
  • DNA (Cytosine-5-)-Methyltransferase 1
  • DNA (Cytosine-5-)-Methyltransferases / chemistry
  • DNA (Cytosine-5-)-Methyltransferases / genetics
  • DNA (Cytosine-5-)-Methyltransferases / metabolism*
  • DNA / chemistry
  • DNA / metabolism
  • DNA Methylation
  • Dinucleoside Phosphates / metabolism
  • Gene Rearrangement
  • Molecular Sequence Data
  • Protein Structure, Tertiary

Substances

  • Dinucleoside Phosphates
  • cytidylyl-3'-5'-guanosine
  • DNA
  • DNA (Cytosine-5-)-Methyltransferase 1
  • DNA (Cytosine-5-)-Methyltransferases