Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

Nature

Volumn 432, Issue 7015, 2004, Pages 406-411

  Huyen, Yentram ^a,b   Zgheib, Omar ^a,b   DiTullio Jr , Richard A ^a,b   Gorgoulis, Vassilis G ^a,c   Zacharatos, Panayotis ^a,c   Petty, Tom J ^a,b   Sheston, Emily A ^a   Mellert, Hestia S ^a   Stavridi, Elena S ^a   Halazonetis, Thanos D ^a,b  

^a WISTAR INSTITUTE   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c UNIVERSITY OF ATHENS MEDICAL SCHOOL   (Greece)

Author keywords

[No Author keywords available]

Indexed keywords

CELLS; DNA; YEAST;

CHROMATIN STRUCTURES; EURKAYOTIC CELLS; METHYLATION;

ENZYMES;

DOUBLE STRANDED DNA; HISTONE H3;

DNA;

ANIMAL CELL; ARTICLE; CHROMATIN STRUCTURE; DNA DAMAGE; DNA STRAND BREAKAGE; GENE TARGETING; GENETIC CONSERVATION; METHYLATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; SENSOR; STRUCTURE ANALYSIS; TANDEM REPEAT; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; BINDING SITES; CELL LINE, TUMOR; CHROMATIN; CONSERVED SEQUENCE; CROSS-LINKING REAGENTS; DNA; DNA DAMAGE; HISTONES; HUMANS; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; LYSINE; METHYLATION; METHYLTRANSFERASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHOSPHOPROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

ANIMALIA; EUKARYOTA; SACCHAROMYCES CEREVISIAE; SACCHAROMYCETALES; SCHIZOSACCHAROMYCES POMBE;

EID: 9244252580     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature03114     Document Type: Article

References (30)

1. Schultz, L. B., Chehab, N. H., Malikzay, A. & Halazonetis, T. D. p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks. J. Cell Biol. 151, 1381-1390 (2000).
2. Xia, Z., Morales, J. C., Durphy, W. G. & Carpenter, P. B. Negative cell cycle regulation and DNA damage-inducible phosphorylation of the BRCT protein 53BP1. J. Biol. Chem. 276, 2708-2718 (2001).
3. Anderson, L., Henderson, C. & Adachi, Y. Phosphorylation and rapid relocalization of 53BP1 to nuclear foci upon DNA damage. Mol. Cell. Biol. 21, 1719-1729 (2001).
4. Rappold, I., Iwabuchi, K., Date, T. & Chen, J. Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways. J. Cell Biol. 153, 613-620 (2001).
5. Mochan, T. A., Venere, M., DiTullio, R. A. Jr & Halazonetis, T. D. 53BP1 and NFBD1/MDC1-Nbs1 function in parallel interacting pathways activating ataxia-telangiectasia mutated (ATM) in response to DNA damage. Cancer Res. 63, 8586-8591 (2003).
6. Ward, I. M., Minn, K., Jorda, K. G. & Chen, J. Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX. J. Biol. Chem. 278, L9579-19582 (2003).
7. Iwabuchi, K. et al. Potential role for 53BP1 in DNA end-joining repair through direct interaction with DNA. J. Biol. Chem. 278, 36487-36495 (2003).
8. Weinert, T. A. & Hartwell, L. H. The RAD9 gene controls the cell cycle response to DNA damage in Saccharomyces cerevisiae. Science 241, 317-322 (1988).
9. Willson, J., Wilson, S., Warr, N. & Watts, F. Z. Isolation and characterization of the Schizosacchromyces pombe rhp9 gene: a gene required for the DNA damage checkpoint but not the replication checkpoint. Nucleic Acids Res. 25, 2138-2146 (1997).
10. Saka, Y., Esashi, F., Matsusaka, T., Mochida, S. & Yanagida, M. Damage and replication checkpoint control in fission yeast is ensured by interactions of Crb2, a protein with BRCT motif, with Cut5 and Chk1. Genes Dev. 11, 3387-3400 (1997).
11. Boulton, S. J. et al. Combined functional genomic maps of the C elegans DNA damage response. Science 295, 127-131 (2002).
12. Charier, G. et al. The tudor tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding. Structure 12, 1551-1562 (2004).
13. Selenko, P. et al. SMN tudor domain structure and its interaction with the Sm proteins. Nature Struct. Biol. 8, 27-31 (2001).
14. Sprangers, R., Groves, M. R., Sinning, I. & Sattler, M. High-resolution X-ray and NMR structures of the SMN Tudor domain: conformational variation in the binding site for symmetrically dimethylated arginine residues. J. Mol. Biol. 327, 507-520 (2003).
15. Theobald, D. L., Mitton-Fry, R. M. & Wuttke, D. S. Nucleic acid recognition by OB-fold proteins. Annu. Rev. Biophys. Biomol. Struct. 32, 115-133 (2003).
16. Friesen, W. J., Massenet, S., Paushkin, S., Wyce, A. & Dreyfuss, G. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell 7, 1111-1117 (2001).
17. Brahms, H., Meheus, L., de Brabandere, V., Fischer, U. & Luhrmann, R. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA 7, 1531-1542 (2001).
18. Kouzarides, T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12, 198-209 (2002).
19. Feng, Q. et al. Methylation of H3-lysine 79 is mediated by a new family of HMTases without a SET domain. Curr. Biol. 12, 1052-1058 (2002).
20. van Leeuwen, F., Gafken, P. R. & Gottschling, D. E. Dot1p modulates silencing in yeast by methylation of the nucleosome core. Cell 109, 745-756 (2002).
21. Lacoste, N., Utley, R. T., Hunter, J. M., Poirier, G. G. & Cote, J. Disrupter of telomeric silencing-1 is a chromatin-specific histone H3 methyltransferase. J. Biol Chem. 277, 30421-30424 (2002).
22. Game, J. C., Williamson M. S. & Baccari, C. X-ray survival characteristics and genetic analysis for nine Saccharomyces deletion mutants that affect radiation sensitivity. Genetics online publication, 15 September 2004 (doi:10.1534/genetics.104.028613).
23. San-Segundo, P. A. & Roeder, G. S. Role for the silencing protein Dot1 in meiotic checkpoint control. Mol. Biol. Cell 11, 3601-3615 (2000).
24. Rogakou, E. P., Boon, C., Redon, C. & Bonner, W. M. Megabase chromatin domains involved in DNA double-strand breaks in vivo. J. Cell Biol. 146, 905-916 (1999).
25. Bakkenist, C. J. & Kastan, M. B. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. Nature 421, 499-506 (2003).
26. Celeste, A. et al. Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks. Nature Cell Biol. 5, 675-679 (2003).
27. Luger, K., Mader, A. W., Richmond, R. K., Sargent, D. F. & Richmond, T. J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389, 251-260 (1997).
28. Mozziconacci, J. & Victor, J. M. Nucleosome gaping supports a functional structure for the 30 nm chromatin fiber. J. Struct. Biol 143, 72-76 (2003).
29. Hyen, Y. et al. Structural differences in the DNA binding domains of human p53 and its C. elegans ortholog Cep-1. Structure 12, 1237-1243 (2004).
30. Kannouche, P. L., Wing, J. & Lehmann, A. R. Interaction of human DNA polymerase ε with monoubiquitinated PCNA: a possible mechanism for the polymerase switch in response to DNA damage. Mol. Cell 14, 491-500 (2004).