Structural studies of the human PBAF chromatin-remodeling complex.
ATP-dependent chromatin remodeling is one of the central processes responsible for imparting fluidity to chromatin and thus regulating DNA transactions. Although knowledge on this process is accumulating rapidly, the basic mechanism (or mechanisms) by which the remodeling complexes alter the structure of a nucleosome is not yet understood. Structural information on these macromolecular machines should aid in interpreting the biochemical and genetic data; to this end, we have determined the structure of the human PBAF ATP-dependent chromatin-remodeling complex preserved in negative stain by electron microscopy and have mapped the nucleosome binding site using two-dimensional (2D) image analysis. PBAF has an overall C-shaped architecture--with a larger density to which two smaller knobs are attached--surrounding a central cavity; one of these knobs appears to be flexible and occupies different positions in each of the structures determined. The 2D analysis of PBAF:nucleosome complexes indicates that the nucleosome binds in the central cavity.
Leschziner
Andres E
AE
Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Lemon
Bryan
B
Tjian
Robert
R
Nogales
Eva
E
D001665:Binding Sites; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D021621:Imaging, Three-Dimensional; D008968:Molecular Conformation; D009707:Nucleosomes / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry* / Q000648:ultrastructure
D002868:Chromosomal Proteins, Non-Histone; D009707:Nucleosomes; C445179:SWI-SNF-B chromatin-remodeling complex; D014157:Transcription Factors