Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.
Molecular architecture of the ATP-dependent chromatin-remodeling complex SWR1.
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DOI:
10.1016/j.cell.2013.08.018
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发表时间:
2013-09-12
期刊:
影响因子:
64.5
通讯作者:
Leschziner AE
中科院分区:
文献类型:
--
作者:
Nguyen VQ;Ranjan A;Stengel F;Wei D;Aebersold R;Wu C;Leschziner AE
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. SWR1 consists of four structurally discrete functional modules Rvb1 and Rvb2 assemble into a single, heterohexameric ring in SWR1 SWR1 undergoes a large conformational change upon nucleosome binding SWR1 forms limited contact with the nucleosome core particle Structural analysis of the 14 subunit SWR1 chromatin remodeler identifies the orientation of its functional modules and reveals conformational changes induced by nucleosome binding.
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DOI:
10.1139/o09-159
发表时间:
2010-02-01
期刊:
BIOCHEMISTRY AND CELL BIOLOGY-BIOCHIMIE ET BIOLOGIE CELLULAIRE
影响因子:
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作者:
Cheung, Kevin L. Y.;Huen, Jennifer;Ortega, Joaquin
通讯作者:
Ortega, Joaquin