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. 2014 Jul 15;28(14):1604–1619. doi: 10.1101/gad.240515.114

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© 2014 Gritenaite 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 1. — An evolutionarily conserved, phosphorylation-dependent interaction between Slx4 and Dpb11/TopBP1. (A) Schematic diagram of Dpb11 domain structure depicted with its interaction partners in replication initiation and DNA damage checkpoint. (B) Slx4 binds to the BRCT3+4 domain of Dpb11. Two-hybrid analysis of GAL4-BD fused to full-length Dpb11 or to BRCT1+2 and BRCT3+4 fragments and of GAL4-AD fusions with Slx4, Rad9, and Ddc1. (C) The Slx4–Dpb11 interaction is reduced by mutation of Slx4 Ser486 and is regulated by DNA damage. Coimmunoprecipitation of endogenous Dpb11 with Slx4^3Flag or phosphorylation-deficient Slx4-S486A^3Flag from undamaged cells or cells treated for 30 min with 0.033% MMS. (D) Human TopBP1 and Slx4 interact dependent on Thr1260 of Slx4. Coimmunoprecipitation of human ^mycTopBP1 with ^GFPSlx4 or N-terminally truncated ^GFPSlx4ΔN after transient overexpression in HEK293T cells. Slx4 or Slx4ΔN was expressed either as wild type (WT) or a T1260A phosphorylation-deficient variant.