Nucleosome sliding by Chd1 does not require rigid coupling between DNA-binding and ATPase domains

Chromatin remodellers are ATP‐dependent motor proteins that physically reposition and reorganize nucleosomes. Chd1 and Iswi‐type remodellers possess a DNA‐binding domain (DBD) needed for efficient nucleosome mobilization; however, it has not been clear how this domain physically contributes to remod...

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Bibliographic Details
Published in:EMBO reports 2013-12, Vol.14 (12), p.1098-1103
Main Authors: Nodelman, Ilana M, Bowman, Gregory D
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - metabolism
Animals
ATP
Binding
Biophysics
Catalytic Domain
Chd1
Chromatin
Chromatin Assembly and Disassembly
chromatin remodeller
Deoxyribonucleic acid
DNA
DNA - metabolism
DNA polymerase
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
EMBO09
Molecular biology
Molecular motors
nucleosome sliding
Nucleosomes
Nucleosomes - chemistry
Nucleosomes - genetics
Nucleosomes - metabolism
Protein Binding
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - metabolism
Scientific Report
Scientific Reports
Sliding
Studies
Substrates
Tethering
Xenopus
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Summary:Chromatin remodellers are ATP‐dependent motor proteins that physically reposition and reorganize nucleosomes. Chd1 and Iswi‐type remodellers possess a DNA‐binding domain (DBD) needed for efficient nucleosome mobilization; however, it has not been clear how this domain physically contributes to remodelling. Here we show that the Chd1 DBD promotes nucleosome sliding simply by tethering the remodeller to nucleosome substrates. Nucleosome sliding activity was largely resistant to increasing length and flexibility of the linker connecting the DBD and ATPase motor, arguing that the ATPase motor does not shift DNA onto the nucleosome by pulling on the DBD. Chromatin remodellers are thought to require a rigid connection between ATPase and DNA‐binding domain to reposition nucleosomes. However, the linking segment of Chd1 can accommodate large changes in length and flexibility, showing that current models for remodeller activity must be revised.
ISSN:1469-221X
1469-3178
DOI:10.1038/embor.2013.158