Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.

@article{Tang2011StructureOT,
  title={Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.},
  author={Yong Tang and Marc A. Holbert and Neda Delgoshaie and Hugo Wurtele and Benoit I Guillemette and Katrina Meeth and Hua Yuan and Paul Drogaris and Eun-Hye Lee and Chantal Durette and Pierre Thibault and Alain Verreault and Philip A Cole and Ronen Marmorstein},
  journal={Structure},
  year={2011},
  volume={19 2},
  pages={221-31}
}
Yeast Rtt109 promotes nucleosome assembly and genome stability by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1. We report the crystal structure of an Rtt109-AcCoA/Vps75 complex revealing an elongated Vps75 homodimer bound to two globular Rtt109 molecules to form a symmetrical holoenzyme with a ∼12 Å diameter central hole. Vps75 and Rtt109 residues that mediate complex formation in the crystals are also important for… CONTINUE READING

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