Abstract
dMi-2, the ATPase subunit of the Drosophila nucleosome remodelling and histone deacetylation (dNuRD) complex, was identified in a two-hybrid screen as an interacting partner of the transcriptional repressor, Tramtrack69 (Ttk69). A short region of Ttk69 is sufficient to mediate this interaction. Ttk69, but not the Ttk88 isoform, co-purifies with the dNuRD complex isolated from embryo extracts. dMi-2 and Ttk69 co-immunoprecipitate from embryonic extracts, indicating that they can associate in vivo. Both dMi-2 and Ttk69 co-localize at a number of discrete sites on polytene chromosomes, showing that they bind common target loci. We also demonstrate that dMi-2 and Ttk interact genetically, indicating a functional interaction in vivo. We propose that Ttk69 represses some target genes by remodelling chromatin structure through the recruitment of the dNuRD complex.
Original language | English |
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Pages (from-to) | 1089-94 |
Number of pages | 6 |
Journal | EMBO Reports |
Volume | 2 |
Issue number | 12 |
DOIs | |
Publication status | Published - Dec 2001 |
Keywords
- Adenosine Triphosphatases
- Animals
- Autoantigens
- Blotting, Western
- Carrier Proteins
- Chromatin
- Drosophila
- Drosophila Proteins
- Gene Expression Regulation
- Histone Deacetylases
- Mi-2 Nucleosome Remodeling and Deacetylase Complex
- Protein Binding
- Protein Subunits
- Repressor Proteins
- Two-Hybrid System Techniques
- Yeasts