Access

You are not currently logged in.

Access your personal account or get JSTOR access through your library or other institution:

login

Log in to your personal account or through your institution.

If You Use a Screen Reader

This content is available through Read Online (Free) program, which relies on page scans. Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.

Interactions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex

Matheshwaran Saravanan, Jochen Wuerges, Daniel Bose, Elizabeth A. McCormack, Nicola J. Cook, Xiaodong Zhang and Dale B. Wigley
Proceedings of the National Academy of Sciences of the United States of America
Vol. 109, No. 51 (December 18, 2012), pp. 20883-20888
Stable URL: http://www.jstor.org/stable/41830634
Page Count: 6
  • Read Online (Free)
  • Subscribe ($19.50)
  • Cite this Item
Since scans are not currently available to screen readers, please contact JSTOR User Support for access. We'll provide a PDF copy for your screen reader.
Interactions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex
Preview not available

Abstract

Actin-related protein Arp8 is a component of the INO80 chromatin remodeling complex. Yeast Arp8 (yArp8) comprises two domains: a 25-KDa N-terminal domain, found only in yeast and a 75-KDa C-terminal domain (yArp8CTD) that contains the actin fold and is conserved across other species. The crystal structure shows that yArp8CTD contains three insertions within the actin core. Using a combination of biochemistry and EM, we show that Arp8 forms a complex with nucleosomes, and that the principal interactions are via the H3 and H4 histones, mediated through one of the yArp8 insertions. We show that recombinant yArp8 exists in monomeric and dimeric states, but the dimer is the biologically relevant form required for stable interactions with histones that exploits the twofold symmetry of the nucleosome core. Taken together, these data provide unique insight into the stoichiometry, architecture, and molecular interactions between components of the INO80 remodeling complex and nucleosomes, providing a first step toward building up the structure of the complex.

Page Thumbnails

  • Thumbnail: Page 
[20883]
    [20883]
  • Thumbnail: Page 
20884
    20884
  • Thumbnail: Page 
20885
    20885
  • Thumbnail: Page 
20886
    20886
  • Thumbnail: Page 
20887
    20887
  • Thumbnail: Page 
20888
    20888