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Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly.

Chromatin assembly factor 1 (CAF-1) and Rtt106 participate in the deposition of newly synthesized histones onto replicating DNA to form nucleosomes. This process is critical for the maintenance of genome stability and inheritance of functionally specialized chromatin structures in proliferating cells. However, the molecular functions of the acetylation of newly synthesized histones in this DNA replication-coupled nucleosome assembly pathway remain enigmatic. Here we show that histone H3 acetylated at lysine 56 (H3K56Ac) is incorporated onto replicating DNA and, by increasing the binding affinity of CAF-1 and Rtt106 for histone H3, H3K56Ac enhances the ability of these histone chaperones to assemble DNA into nucleosomes. Genetic analysis indicates that H3K56Ac acts in a nonredundant manner with the acetylation of the N-terminal residues of H3 and H4 in nucleosome assembly. These results reveal a mechanism by which H3K56Ac regulates replication-coupled nucleosome assembly mediated by CAF-1 and Rtt106.

Pubmed ID: 18662540


  • Li Q
  • Zhou H
  • Wurtele H
  • Davies B
  • Horazdovsky B
  • Verreault A
  • Zhang Z



Publication Data

July 25, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM072719
  • Agency: NIGMS NIH HHS, Id: R01 GM072719-03
  • Agency: NIGMS NIH HHS, Id: R01 GM081838
  • Agency: NIGMS NIH HHS, Id: R01 GM081838-01A1

Mesh Terms

  • Acetylation
  • DNA Damage
  • DNA Replication
  • DNA, Fungal
  • Histones
  • Humans
  • Lysine
  • Molecular Chaperones
  • Mutation
  • Nucleosomes
  • Protein Structure, Tertiary
  • Ribonucleases
  • S Phase
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins