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TitleInteractions between the nucleosome histone core and Arp8 in the INO80 chromatin remodeling complex.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 109, Issue 51, Page 20883-20888, Year 2012
Publish dateDec 18, 2012
AuthorsMatheshwaran Saravanan / Jochen Wuerges / Daniel Bose / Elizabeth A McCormack / Nicola J Cook / Xiaodong Zhang / Dale B Wigley /
PubMed AbstractActin-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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:23213201 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.7 - 22.0 Å
Structure data

EMDB-2224:
Negative stain microscopy of a dimer of Actin-related protein 8 (Arp8) from S. cerevisiae.
Method: EM (single particle) / Resolution: 22.0 Å

EMDB-2225:
Negative stain microscopy of two Actin-related protein 8 (Arp8) molecules from S. cerevisiae bound to a mono-nucleosome.
Method: EM (single particle) / Resolution: 21.0 Å

PDB-4am6:
C-TERMINAL DOMAIN OF ACTIN-RELATED PROTEIN ARP8 FROM S. CEREVISIAE
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-4am7:
ADP-BOUND C-TERMINAL DOMAIN OF ACTIN-RELATED PROTEIN ARP8 FROM S. CEREVISIAE
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsNUCLEAR PROTEIN / CHROMATIN REMODELLING COMPLEX / ATP-BINDING PROTEIN / NUCLEAR ACTIN-RELATED PROTEIN / TRANSCRIPTION REGULATION / DNA REPAIR

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