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Background  Methyl-DNA binding proteins help to translate epigenetic information encoded by DNA methylation into covalent histone modifications.  MBD2/3  is the only candidate gene in the  Drosophila  genome with extended homologies to mammalian MBD2 and MBD3 proteins, which represent a co-repressor and an integral component of the  N ucleosome  R emodelling and  D eacetylase (NuRD) complex, respectively. An association of  Drosophila  MBD2/3 with the  Drosophila  NuRD complex has been suggested previously. We have now analyzed the molecular interactions between MBD2/3 and the NuRD complex in greater detail.    Results  The two MBD2/3 isoforms precisely cofractionated with NuRD proteins during gel filtration of extracts derived from early and late embryos. In addition, we demonstrate that MBD2/3 forms multimers, and engages in specific interactions with the p55 and MI-2 subunits of the  Drosophila  NuRD complex.    Conclusion  Our data provide novel insights into the association between  Drosophila  MBD2/3 and NuRD proteins. Additionally, this work provides a first analysis of the architecture of the  Drosophila  NuRD complex.

The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2.