Decoupling nucleosome recognition from DNA binding dramatically alters the properties of the Chd1 chromatin remodeler
| Autor: | Ashok Kumar Patel, Jeffrey N. McKnight, Gregory D. Bowman, Srinivas Chakravarthy, Seamus Morrone, Ilana M. Nodelman |
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| Rok vydání: | 2012 |
| Předmět: |
Histone-modifying enzymes
Saccharomyces cerevisiae Proteins Recombinant Fusion Proteins Solenoid (DNA) Gene Regulation Chromatin and Epigenetics DNA-binding protein Chromatin remodeling Histones 03 medical and health sciences 0302 clinical medicine Genetics Nucleosome 030304 developmental biology 0303 health sciences biology DNA Chromatin Assembly and Disassembly Molecular biology Chromatin Nucleosomes Protein Structure Tertiary Cell biology DNA-Binding Proteins Histone biology.protein DNA supercoil Streptavidin 030217 neurology & neurosurgery |
| Zdroj: | Nucleic Acids Research |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/gks1440 |
| Popis: | Chromatin remodelers can either organize or disrupt nucleosomal arrays, yet the mechanisms specifying these opposing actions are not clear. Here, we show that the outcome of nucleosome sliding by Chd1 changes dramatically depending on how the chromatin remodeler is targeted to nucleosomes. Using a Chd1–streptavidin fusion remodeler, we found that targeting via biotinylated DNA resulted in directional sliding towards the recruitment site, whereas targeting via biotinylated histones produced a distribution of nucleosome positions. Remarkably, the fusion remodeler shifted nucleosomes with biotinylated histones up to 50 bp off the ends of DNA and was capable of reducing negative supercoiling of plasmids containing biotinylated chromatin, similar to remodelling characteristics observed for SWI/SNF-type remodelers. These data suggest that forming a stable attachment to nucleosomes via histones, and thus lacking sensitivity to extranucleosomal DNA, seems to be sufficient for allowing a chromatin remodeler to possess SWI/SNF-like disruptive properties. |
| Databáze: | OpenAIRE |
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