title: Nucleosome sliding by Chd1 does not require rigid coupling between DNA-binding and ATPase domains.
abstract: 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.
authors.affiliation: T.C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, MD 21218, USA.
authors.forename: Ilana M
authors.initials: IM
authors.lastname: Nodelman
authors.forename: Gregory D
authors.initials: GD
authors.lastname: Bowman
mesh_terms: D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D020134:Catalytic Domain; D042002:Chromatin Assembly and Disassembly; D004247:DNA / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D009707:Nucleosomes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D014981:Xenopus
chemical_list: C489847:CHD1 protein, S cerevisiae; D004268:DNA-Binding Proteins; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D004247:DNA; D000251:Adenosine Triphosphatases