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Nat Commun. 2015 May 12;6:7108. doi: 10.1038/ncomms8108.

Structural analyses of the chromatin remodelling enzymes INO80-C and SWR-C.

Author information

1
Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, Maasachusetts 01605, USA.
2
1] Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA [2] Howard Hughes Medical Institute, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
3
Stowers Institute for Medical Research, 1000 E 50th Street, Kansas, Missouri 64110, USA.
4
1] Stowers Institute for Medical Research, 1000 E 50th Street, Kansas, Missouri 64110, USA [2] Departments of Pathology and Laboratory Medicine, University of Kansas Medical Center, Kansas, Kansas 66160, USA.
5
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.

Abstract

INO80-C and SWR-C are conserved members of a subfamily of ATP-dependent chromatin remodelling enzymes that function in transcription and genome-maintenance pathways. A crucial role for these enzymes is to control chromosomal distribution of the H2A.Z histone variant. Here we use electron microscopy (EM) and two-dimensional class averaging to demonstrate that these remodelling enzymes have similar overall architectures. Each enzyme is characterized by a dynamic 'tail' domain and a compact 'head' that contains Rvb1/Rvb2 subunits organized as hexameric rings. EM class averages and mass spectrometry support the existence of single heterohexameric rings in both SWR-C and INO80-C. EM studies define the position of the Arp8/Arp4/Act1 module within INO80-C, and we find that this module enhances nucleosome-binding affinity but is largely dispensable for remodelling activities. In contrast, the Ies6/Arp5 module is essential for INO80-C remodelling, and furthermore this module controls conformational changes that may couple nucleosome binding to remodelling.

PMID:
25964121
PMCID:
PMC4431590
DOI:
10.1038/ncomms8108
[Indexed for MEDLINE]
Free PMC Article

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