Tudor domains track down dna breaks

How do cells track down the occasional lesion among the billons of base pairs of chromosomal DNA? A surprising discovery unravels a potential new mechanism: the Tudor domains of the

DNA-damage response factor 53BP1 interact with methylated histones that are likely to become exposed during local chromatin relaxation at sites of DNA double-strand breaks. Access through

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REFERENCES * Celeste, A. et al. Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks. _Nature Cell Biol._ 5, 675–679 (2003). Article  CAS  Google Scholar  *

Huyen, Y. et al. Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks. _Nature_ 432, 406–411 (2004). Article  CAS  Google Scholar  * Charier, G. et al. The Tudor

tandem of 53BP1: a new structural motif involved in DNA and RG-rich peptide binding. _Structure (Camb.)_ 12, 1551–1562 (2004). Article  CAS  Google Scholar  * Bakkenist, C. J. & Kastan,

M. B. DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation. _Nature_ 421, 499–506 (2003). Article  CAS  Google Scholar  * Wang, B., Matsuoka, S.,

Carpenter, P. B. & Elledge, S. J. 53BP1, a mediator of the DNA damage checkpoint. _Science_ 298, 1435–1438 (2002). Article  CAS  Google Scholar  * DiTullio, R. A., Jr. et al. 53BP1

functions in an ATM-dependent checkpoint pathway that is constitutively activated in human cancer. _Nature Cell Biol._ 4, 998–1002 (2002). Article  CAS  Google Scholar  *

Fernandez-Capetillo, O. et al. DNA damage-induced G2–M checkpoint activation by histone H2AX and 53BP1. _Nature Cell Biol._ 4, 993–997 (2002). Article  CAS  Google Scholar  * 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). CAS  PubMed  Google Scholar  * Uziel, T. et al. Requirement of the MRN complex for ATM activation by DNA damage. _EMBO J._ 22, 5612–5621

(2003). Article  CAS  Google Scholar  * de Jager, M. et al. Human Rad50/Mre11 is a flexible complex that can tether DNA ends. _Mol. Cell_ 8, 1129–1135 (2001). Article  CAS  Google Scholar  *

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_

DOI: 10.1534/genetics.104.028613 (2004). * Sanders, S. L. et al. Methylation of histone H4 lysine 20 controls recruitment of Crb2 to sites of DNA damage. _Cell_ DOI:

10.1016/S0092867404010530 (2004). Download references AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * the The Wellcome Trust/Cancer Research UK Gurdon Institute, The Henry Wellcome Building of

Cancer and Developmental Biology, Tennis Court Road, Cambridge, CB2 1QN, UK Manuel Stucki & Stephen P. Jackson Authors * Manuel Stucki View author publications You can also search for

this author inPubMed Google Scholar * Stephen P. Jackson View author publications You can also search for this author inPubMed Google Scholar RIGHTS AND PERMISSIONS Reprints and permissions

ABOUT THIS ARTICLE CITE THIS ARTICLE Stucki, M., Jackson, S. Tudor domains track down DNA breaks. _Nat Cell Biol_ 6, 1150–1152 (2004). https://doi.org/10.1038/ncb1204-1150 Download citation

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