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TitleMolecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.
Journal, issue, pagesCell, Vol. 154, Issue 6, Page 1220-1231, Year 2013
Publish dateSep 12, 2013
AuthorsVu Q Nguyen / Anand Ranjan / Florian Stengel / Debbie Wei / Ruedi Aebersold / Carl Wu / Andres E Leschziner /
PubMed AbstractThe ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone H2A.Z/H2B dimer for a canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters. This ...The ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone H2A.Z/H2B dimer 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.
External linksCell / PubMed:24034246 / PubMed Central
MethodsEM (single particle)
Resolution28.0 - 34.0 Å
Structure data

EMDB-5626:
Molecular Architecture of the ATP-Dependent Chromatin Remodeling Complex SWR1 by 3 Dimensional Electron Microscopy
Method: EM (single particle) / Resolution: 28.0 Å

EMDB-5638:
3D Cryo-negative EM structure of nucleosome-bound SWR1
Method: EM (single particle) / Resolution: 34.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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