Search Organism: All OrganismsArabidopsis thalianaBacillus subtilis 168Bos taurusCaenorhabditis elegansCanis familiarisDanio rerioDrosophila melanogasterEquus caballusEscherichia coli K12Gallus gallusHomo sapiensMacaca mulattaMus musculusNematostella vectensisOryza sativaPan troglodytesRattus norvegicusSaccharomyces cerevisiaeSchizosaccharomyces pombeStrongylocentrotus purpuratusTakifugu rubripesXenopus laevis home help / support contribute downloads mirrors about us J. Biol. Chem. Feb (2008); 283(8):5058-68 Structural and Functional Analysis of the Spt16p N-terminal Domain Reveals Overlapping Roles of yFACT Subunits- Vandemark AP, Xin H, McCullough L, Rawlins R, Bentley S, Heroux A, Stillman DJ, Hill CP, Formosa T Departments of Biochemistry and Pathology, University of Utah School of Medicine, Salt Lake City, Utah 84112 and Biology Department, Brookhaven National Laboratory, Upton, New York 11973- Abstract: yFACT -heterodimers of Saccharomyces cerevisiae Spt16-Pob3 combined with Nhp6- binds to and alters the properties of nucleosomes- The essential function of yFACT is not disrupted by deletion of the N-terminal domain -NTD- of Spt16 or by mutation of the middle domain of Pob3, but either alteration makes yeast cells sensitive to DNA replication stress- We have determined the structure of the Spt16 NTD and find evidence for a conserved potential peptide-binding site- Pob3-M also contains a putative binding site, and we show that these two sites perform an overlapping essential function- We find that yFACT can bind the N-terminal tails of some histones and that this interaction is important for yFACT-nucleosome binding- However, neither the Spt16 NTD nor a key residue in the putative Pob3-M-binding site was required for interactions with histone N termini or for yFACT-mediated nucleosome reorganization in vitro- Instead, both potential binding sites interact functionally with the C-terminal docking domain of the histone H2A- yFACT therefore appears to make multiple contacts with different sites within nucleosomes, and these interactions are partially redundant with one another- The docking domain of H2A is identified as an important participant in maintaining stability during yFACT-mediated nucleosome reorganization, suggesting new models for the mechanism of this activity- [PUBMED: 18089575] Copyright © 2009, Tyers Lab, The Samuel Lunenfeld Research Institute, Mount Sinai Hospital, All Rights Reserved. terms and conditions - privacy policy - Osprey Network Visualization System BioGRID: A General Repository for Interaction Datasets. Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers. Nucleic Acids Res. Jan 1;34:D535-9.