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. 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.
| Item Type: | Journal article |
|---|---|
| Form of publication: | Publisher's Version |
| Faculties: | Medicine > Adolf Butenandt Institute |
| Subjects: | 500 Science > 570 Life sciences; biology |
| URN: | urn:nbn:de:bvb:19-epub-23782-7 |
| ISSN: | 1471-2199 |
| Language: | English |
| Item ID: | 23782 |
| Date Deposited: | 06. Mar 2015 11:20 |
| Last Modified: | 04. Nov 2020 13:05 |

