Structural analysis of the yeast SWI/SNF chromatin remodeling complex.
Elucidating the mechanism of ATP-dependent chromatin remodeling is one of the largest challenges in the field of gene regulation. One of the missing pieces in understanding this process is detailed structural information on the enzymes that catalyze the remodeling reactions. Here we use a combination of subunit radio-iodination and scanning transmission electron microscopy to determine the subunit stoichiometry and native molecular weight of the yeast SWI/SNF complex. We also report a three-dimensional reconstruction of yeast SWI/SNF derived from electron micrographs.
Smith
Corey L
CL
University of Massachusetts Medical School, Program in Molecular Medicine, Worcester 01605, USA.
Horowitz-Scherer
Rachel
R
Flanagan
Joan F
JF
Woodcock
Christopher L
CL
Peterson
Craig L
CL
D000251:Adenosine Triphosphatases; D002843:Chromatin / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D007091:Image Processing, Computer-Assisted; D007457:Iodine Radioisotopes; D046911:Macromolecular Substances; D017348:Microscopy, Electron, Scanning Transmission; D008958:Models, Molecular; D008970:Molecular Weight; D009687:Nuclear Proteins; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000378:metabolism; 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; D007457:Iodine Radioisotopes; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D000251:Adenosine Triphosphatases; C499333:SNF2 protein, S cerevisiae