Histone Peptide Array identifies DNMT interactions

A group of researchers, led by Albert Jeltsch, managed to provide the first evidence that preferential binding of a DNA methyltransferases to histone tails carrying specific modification patterns directly leads to the favored methylation of DNA bound to the modified chromatin. Using peptide arrays the researchers showed that this effect can be achieved by the ADD domain of Dnmt3a, which specifically interacts with the H3 histone 1-19 tail. The binding is disrupted by several post-translational modifications on the histone H3 tail (K4me2/me3/ac, T3ph, S10ph and T11ph). To establish a functional role of the ADD domain binding to unmodified H3 tails, the DNA methylation of in vitroreconstituted chromatin with Dnmt3a was analyzed. Chromatin substrates with unmodified H3 tail or with H3K9me3 modification were methylated more efficiently by full-length Dnmt3a than chromatin trimethylated at H3K4. These results demonstrate that the binding of the ADD domain to H3 tails unmethylated at K4 leads to the preferential methylation of DNA bound to chromatin with this modification state.
See Zhang et al. (2010) Nucleic Acids Res. 2010, Mar 11. Abstract.

Data in this paper were generated in part using Active Motif's MODified™ Histone Peptide Arrays* (Catalog No. 13001).
*CelluSpots™ arrays are manufactured under license by INTAVIS Bioanalytical Instruments AG and sold through Active Motif as MODified™ Histone Peptide Arrays.

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