Structural analyses of the chromatin remodeling enzymes INO80-C and SWR-C
Washburn, Michael P.
Hong, Eun-Jin Erica
Peterson, Craig L.
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CitationWatanabe, Shinya, Dongyan Tan, Mahadevan Lakshminarasimhan, Michael P. Washburn, Eun-Jin Erica Hong, Thomas Walz, and Craig L. Peterson. 2015. “Structural analyses of the chromatin remodeling enzymes INO80-C and SWR-C.” Nature communications 6 (1): 7108. doi:10.1038/ncomms8108. http://dx.doi.org/10.1038/ncomms8108.
AbstractINO80-C and SWR-C are conserved members of a subfamily of ATP-dependent chromatin remodeling 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 (2D) class averaging to demonstrate that these remodeling 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 remodeling activities. In contrast, the Ies6/Arp5 module is essential for INO80-C remodeling, and furthermore this module controls conformational changes that may couple nucleosome binding to remodeling.
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