Molecular Biology

Open to Repair

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Science  09 Aug 2013:
Vol. 341, Issue 6146, pp. 593
DOI: 10.1126/science.341.6146.593-b

The information stored in DNA underpins almost all life. It is therefore not surprising that there are multiple systems for rapidly sensing and repairing damage to genomic DNA within cells. The repair systems in eukaryotic cells have necessarily had to evolve to be able to correct such damage in the context of the chromatin proteins—principally histones—that compact DNA in the nucleus. Toiber et al. have studied the role of the SIRT6 histone deacetylase in the response of mammalian tissue culture cells to double-strand breaks in DNA. They find that SIRT6, which can bind to chromatin, interacts with the histone remodeling protein SNF2H and recruits it to sites of double-strand DNA breaks. The dual abilities of SIRT6 to deacetylate histone H3 at lysine 56 and to recruit SNF2H are necessary for DNA repair to occur and provide further evidence that remodeling chromatin to allow access by the repair machinery is critical for an effective DNA damage response. Both proteins act in the same DNA repair pathway, and their interaction shows tissue specificity, in the pancreas and brain, possibly consistent with the role of SIRT6 in brain function.

Mol. Cell 51, 10.1016/j.molcel.2013.06.018 (2013).

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