Structural analysis of the RSC chromatin-remodeling complex.
Electron microscopy of the RSC chromatin-remodeling complex reveals a ring of protein densities around a central cavity. The size and shape of the cavity correspond closely to those of a nucleosome. Results of nuclease protection analysis are consistent with nucleosome binding in the cavity. Such binding could explain the ability of RSC to expose nucleosomal DNA in the presence of ATP without loss of associated histones.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002843:Chromatin / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D006657:Histones / Q000378:metabolism; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D008854:Microscopy, Electron; D015394:Molecular Structure; D009707:Nucleosomes / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D051381:Rats; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*
D002843:Chromatin; D004268:DNA-Binding Proteins; D006657:Histones; D046911:Macromolecular Substances; D009707:Nucleosomes; C103337:RSC complex, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D000255:Adenosine Triphosphate