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.
MeSH Terms
Adenosine Triphosphatases
Animals
Autoantigens/genetics,metabolism
Blotting, Western
Carrier Proteins/genetics,metabolism
Chromatin/chemistry,genetics,metabolism
Drosophila/genetics,metabolism
Drosophila Proteins
Gene Expression Regulation
Histone Deacetylases/chemistry,metabolism
Mi-2 Nucleosome Remodeling and Deacetylase Complex
Protein Binding
Protein Subunits
Repressor Proteins/genetics,metabolism
Two-Hybrid System Techniques
Yeasts
Chemicals
Autoantigens
Carrier Proteins
Chromatin
Drosophila Proteins
Mi-2 protein, Drosophila
Protein Subunits
Repressor Proteins
ttk protein, Drosophila
Histone Deacetylases
Mi-2 Nucleosome Remodeling and Deacetylase Complex
Adenosine Triphosphatases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Murawsky C M
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Brehm A
Badenhorst P
Lowe N
Becker P B
Travers A A
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