The Drosophila methyl-DNA binding protein MBD2/3 interacts with the NuRD complex via p55 and MI-2
| Autor: | Kramer Katja, Brehm Alexander, Marhold Joachim |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
Adenosine Triphosphatases
lcsh:QH426-470 lcsh:Cytology Chromosomal Proteins Non-Histone Autoantigens Histone Deacetylases DNA-Binding Proteins lcsh:Genetics Two-Hybrid System Techniques Animals Drosophila Proteins Protein Isoforms Drosophila Retinoblastoma-Binding Protein 4 lcsh:QH573-671 Mi-2 Nucleosome Remodeling and Deacetylase Complex Molecular Chaperones Research Article |
| Zdroj: | BMC Molecular Biology BMC Molecular Biology, Vol 5, Iss 1, p 20 (2004) |
| ISSN: | 1471-2199 |
| Popis: | 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. 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full text from SpringerLink