title: The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2.
abstract: 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 Nucleosome Remodelling and Deacetylase (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.
  
  
  CONCLUSIONS
  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.
authors.affiliation: Research Group Epigenetics, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 580, 69120 Heidelberg, Germany. j.marhold@dkfz.de
authors.forename: Joachim
authors.initials: J
authors.lastname: Marhold
authors.forename: Alexander
authors.initials: A
authors.lastname: Brehm
authors.forename: Katja
authors.initials: K
authors.lastname: Kramer
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D001324:Autoantigens / Q000378:metabolism*; D002868:Chromosomal Proteins, Non-Histone / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000302:isolation & purification / Q000378:metabolism*; D004330:Drosophila / Q000196:embryology / Q000378:metabolism; D029721:Drosophila Proteins / Q000378:metabolism*; D006655:Histone Deacetylases / Q000378:metabolism*; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex; D018832:Molecular Chaperones / Q000378:metabolism*; D020033:Protein Isoforms / Q000378:metabolism; D056505:Retinoblastoma-Binding Protein 4; D020798:Two-Hybrid System Techniques
chemical_list: D001324:Autoantigens; C110251:Caf1-55 protein, Drosophila; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; C115368:MBD2 protein; C116095:Mi-2 protein, Drosophila; D018832:Molecular Chaperones; D020033:Protein Isoforms; D056505:Retinoblastoma-Binding Protein 4; D006655:Histone Deacetylases; D056245:Mi-2 Nucleosome Remodeling and Deacetylase Complex; D000251:Adenosine Triphosphatases