Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.
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.
Mesh Terms:
Adenosine Triphosphatases, Chromatin Assembly and Disassembly, DNA Helicases, Dimerization, Multiprotein Complexes, Nucleosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Adenosine Triphosphatases, Chromatin Assembly and Disassembly, DNA Helicases, Dimerization, Multiprotein Complexes, Nucleosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors
Cell
Date: Sep. 12, 2013
PubMed ID: 24034246
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