@article {6413,
	title = {Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.},
	journal = {Cell},
	volume = {154},
	year = {2013},
	month = {2013 Sep 12},
	pages = {1220-31},
	abstract = {<p>The ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone H2A.Z/H2B dimer\&nbsp;for a canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters. This localization of H2A.Z is conserved throughout eukaryotes. SWR1 is a 1 megadalton complex containing 14 different polypeptides, including the AAA+ ATPases Rvb1 and Rvb2. Using electron microscopy, we obtained the three-dimensional structure of SWR1 and mapped its major functional components. Our data show that SWR1 contains a single heterohexameric Rvb1/Rvb2 ring that, together with the catalytic subunit Swr1, brackets two independently assembled multisubunit modules. We also show that SWR1 undergoes a large conformational change upon engaging a limited region of the nucleosome core particle. Our work suggests an important structural role for the Rvbs and a distinct substrate-handling mode by SWR1, thereby providing a structural framework for understanding the complex dimer-exchange reaction.</p>
},
	issn = {1097-4172},
	doi = {10.1016/j.cell.2013.08.018},
	author = {Nguyen, Vu Q and Ranjan, Anand and Stengel, Florian and Wei, Debbie and Aebersold, Ruedi and Wu, Carl and Leschziner, Andres E}
}
@article {2415,
	title = {Structural studies of the human PBAF chromatin-remodeling complex.},
	journal = {Structure},
	volume = {13},
	year = {2005},
	month = {2005 Feb},
	pages = {267-75},
	abstract = {<p>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{\textendash}with a larger density to which two smaller knobs are attached{\textendash}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.</p>
},
	keywords = {Binding Sites, Chromosomal Proteins, Humans, Imaging, Molecular Conformation, Non-Histone, Nucleosomes, Three-Dimensional, Transcription Factors},
	issn = {0969-2126},
	doi = {10.1073/pnas.1100640108},
	author = {Leschziner, Andres E and Lemon, Bryan and Tjian, Robert and Nogales, Eva}
}
