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. 2016 May 15;30(10):1211–1224. doi: 10.1101/gad.280685.116

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© 2016 Tsabar et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 7. — A model for the role of Asf1 in the dynamic sensing of DNA damage. After a Ddc2–Mec1 recognizes a DSB, Mec1 phosphorylates Rad53, leading to Rad53 dissociation from Asf1. Rad53 then undergoes hyperphosphorylation. PP2C dephosphorylates Rad53, and the dephosphorylated Rad53 reassociates with Asf1. If the damage persists, Mec1 can rephosphorylate Rad53 and lead to dissociation from Asf1 and reactivation. In addition, activated Rad53 can counter the dephosphorylation by autophosphorylation. In parallel, Asf1-bound histone H3 undergoes modifications by Rtt109 and Rtt101, which facilitate the handoff of the H3–H4 histone dimer to CAF-1, freeing Asf1 to reinteract with Rad53.