Rtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication

@article{Han2007Rtt109AH,
  title={Rtt109 Acetylates Histone H3 Lysine 56 and Functions in DNA Replication},
  author={Junhong Han and Hui Zhou and Bruce F. Horazdovsky and Kangling Zhang and Rui-Ming Xu and Zhiguo Zhang},
  journal={Science},
  year={2007},
  volume={315},
  pages={653 - 655}
}
Acetylation of histone H3 lysine 56 (H3-K56) occurs in S phase, and cells lacking H3-K56 acetylation are sensitive to DNA-damaging agents. However, the histone acetyltransferase (HAT) that catalyzes global H3-K56 acetylation has not been found. Here we show that regulation of Ty1 transposition gene product 109 (Rtt109) is an H3-K56 HAT. Cells lacking Rtt109 or expressing rtt109 mutants with alterations at a conserved aspartate residue lose H3-K56 acetylation and exhibit increased sensitivity… 
Histone H3-K56 acetylation is important for genomic stability in mammals
TLDR
It is shown that proper H3K56 acetylation is critical for genomic stability and DNA damage response and two regulators of this modification are identified.
Regulation of Histone H3 Lysine 56 Acetylation in Schizosaccharomyces pombe*
TLDR
Both the regulation of histone H3 Lys-56 acetylation by its histone acetyltransferase and histone deacetylase and its role in the DNA damage response are conserved among two distantly related yeast model organisms.
Acetylation of Lysine 56 of Histone H3 Catalyzed by RTT109 and Regulated by ASF1 Is Required for Replisome Integrity*
TLDR
It is shown that cells lacking Rtt109 or expressing H3-K56 mutants exhibited significant reduction in the association of three proteins with stalled DNA replication forks and hyper-recombination of replication forks stalled at replication fork barriers of the ribosomal DNA locus compared with wild-type cells.
Histone H3-K56 acetylation is catalyzed by histone chaperone-dependent complexes.
Histone H3 K56 acetylation, chromatin assembly, and the DNA damage checkpoint.
  • J. Downs
  • Biology, Chemistry
    DNA repair
  • 2008
Chaperone Control of the Activity and Specificity of the Histone H3 Acetyltransferase Rtt109
TLDR
A whole-genome screen to identify genes whose deletions have synthetic genetic interactions with rtt109Δ suggests Rtt109 has functions in addition to DNA repair, and it is shown that Rtt 109 and Gcn5 are the only H3-K9 HATs in vivo, and another histone chaperone, Asf1, and Vps75 are both required for acetylation of lysine 9 on H3 in vivo.
The Rtt109-Vps75 Histone Acetyltransferase Complex Acetylates Non-nucleosomal Histone H3*
TLDR
Insight is provided into how H3-Lys-56 acetylation is regulated during the cell cycle by showing that Rtt109 forms a complex with Vps75 and that both recombinant Rtt 109-Vps75 complexes and native complexes purified from yeast cells acetylate H3 present in H3/H4/ H2A/H2B core histones but not other histones.
Multisite Substrate Recognition in Asf1-Dependent Acetylation of Histone H3 K56 by Rtt109
Sites of Acetylation on Newly Synthesized Histone H4 Are Required for Chromatin Assembly and DNA Damage Response Signaling
TLDR
The results indicate that the sites of acetylation on newly synthesized histones H3 and H4 can function in nonoverlapping ways that are required for chromatin assembly, viability, and DNA damage response signaling.
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