CoChat
Sign Up
Cited by 544

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response

Masumoto, Hiroshi, Hawke, David, Kobayashi, Ryuji, Verreault, Alain·2005·Nature
DOI 10.1038/nature03714
Open this paper in CoChat — free account

Abstract

DNA breaks are extremely harmful lesions that need to be repaired efficiently throughout the genome. However, the packaging of DNA into nucleosomes is a significant barrier to DNA repair, and the mechanisms of repair in the context of chromatin are poorly understood. Here we show that lysine 56 (K56) acetylation is an abundant modification of newly synthesized histone H3 molecules that are incorporated into chromosomes during S phase. Defects in the acetylation of K56 in histone H3 result in sensitivity to genotoxic agents that cause DNA strand breaks during replication. In the absence of DNA damage, the acetylation of histone H3 K56 largely disappears in G2. In contrast, cells with DNA breaks maintain high levels of acetylation, and the persistence of the modification is dependent on DNA damage checkpoint proteins. We suggest that the acetylation of histone H3 K56 creates a favourable chromatin environment for DNA repair and that a key component of the DNA damage response is to preserve this acetylation.

Overview

Integrity signals

Registry

Crossref · 10.1038/nature03714

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Show all 1 references

Research works printed but not linked: 20

  1. Peterson, C. L. & Côté, J. Cellular machineries for chromosomal DNA repair. Genes Dev. 18, 602–616 (2004) · DOI
  2. Sklenar, A. R. & Parthun, M. R. Characterization of yeast histone H3-specific type B histone acetyltransferases identifies an ADA2-independent Gcn5p activity. BMC Biochem. 5, 1–12 (2004) · DOI
  3. Ye, J. et al. Histone H4 lysine 91 acetylation: A core domain modification associated with chromatin assembly. Mol. Cell 18, 123–130 (2005) · DOI
  4. Verreault, A., Kaufman, P. D., Kobayashi, R. & Stillman, B. Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4. Cell 87, 95–104 (1996) · DOI
  5. Gunjan, A. & Verreault, A. A Rad53 kinase-dependent surveillance mechanism that regulates histone protein levels in S. cerevisiae. Cell 115, 537–549 (2003) · DOI
  6. Downs, J. A., Lowndes, N. F. & Jackson, S. P. A role for Saccharomyces cerevisiae histone H2A in DNA repair. Nature 408, 1001–1004 (2000) · DOI
  7. Redon, C. et al. Yeast histone 2A serine 129 is essential for the efficient repair of checkpoint-blind DNA damage. EMBO Rep. 4, 678–684 (2003) · DOI
  8. Pilch, D. R. et al. Characteristics of γ-H2AX foci at DNA double-strand break sites. Biochem. Cell Biol. 81, 123–129 (2003) · DOI
  9. Bird, A. W. et al. Acetylation of histone H4 by Esa1 is required for DNA double-strand break repair. Nature 419, 411–415 (2002) · DOI
  10. Haber, J. E. Partners and pathways: repairing a double-strand break. Trends Genet. 16, 259–264 (2000) · DOI
  11. Pommier, Y. et al. Repair of and checkpoint response to topoisomerase I-mediated DNA damage. Mutat. Res. 532, 173–203 (2003) · DOI
  12. Hsiang, Y. H., Lihou, M. G. & Liu, L. F. Arrest of replication forks by drug-stabilized topoisomerase I-DNA cleavable complexes as a mechanism of cell killing by camptothecin. Cancer Res. 49, 5077–5082 (1989)
  13. Nitiss, J. L. & Wang, J. C. Mechanisms of cell killing by drugs that trap covalent complexes between DNA topoisomerases and DNA. Mol. Pharmacol. 50, 1095–1102 (1996)
  14. Tercero, J. A., Longhese, M. P. & Diffley, J. F. X. A central role for DNA replication forks in checkpoint activation and response. Mol. Cell 11, 1323–1326 (2003) · DOI
  15. Davey, C. A., Sargent, D. F., Luger, K., Maeder, A. W. & Richmond, T. J. Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution. J. Mol. Biol. 319, 1097–1113 (2002) · DOI
  16. Norton, V. G., Imai, B. S., Yau, P. & Bradbury, E. M. Histone acetylation reduces nucleosome core particle linking number change. Cell 57, 449–457 (1989) · DOI
  17. Wechser, M. A., Kladde, M. P., Alfieri, J. A. & Peterson, C. L. Effects of Sin- versions of histone H4 on yeast chromatin structure and function. EMBO J. 16, 2086–2095 (1997) · DOI
  18. Sogo, J. M., Stahl, H., Koller, T. & Knippers, R. Structure of replicating simian virus 40 minichromosomes. The replication fork, core histone segregation and terminal structures. J. Mol. Biol. 189, 189–204 (1986) · DOI
  19. Downs, J. A. et al. Binding of chromatin-modifying activities to phosphorylated histone H2A at DNA damage sites. Mol. Cell 16, 979–990 (2004) · DOI
  20. Kushnirov, V. V. Rapid and reliable protein extraction from yeast. Yeast 16, 857–860 (2000) · DOI

Cited by

Sorted by citations

Metadata

Authors
Masumoto, H., Hawke, D., Kobayashi, R., & Verreault, A.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2005-07
Volume
436
Issue
7048
Pages
294-298
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/nature03714
Cited by
544
References
1
Language
en
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review