Reference: Wade BO, et al. (2017) Structural studies of RFC(C)(tf18) reveal a novel chromatin recruitment role for Dcc1. EMBO Rep 18(4): 558-568.

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Abstract


Replication factor C complexes load and unload processivity clamps from DNA and are involved in multiple DNA replication and repair pathways. The RFC(C)(tf18) variant complex is required for activation of the intra-S-phase checkpoint at stalled replication forks and aids the establishment of sister chromatid cohesion. Unlike other RFC complexes, RFC(C)(tf18) contains two non-Rfc subunits, Dcc1 and Ctf8. Here, we present the crystal structure of the Dcc1-Ctf8 heterodimer bound to the C-terminus of Ctf18. We find that the C-terminus of Dcc1 contains three-winged helix domains, which bind to both ssDNA and dsDNA We further show that these domains are required for full recruitment of the complex to chromatin, and correct activation of the replication checkpoint. These findings provide the first structural data on a eukaryotic seven-subunit clamp loader and define a new biochemical activity for Dcc1.

Reference Type
Journal Article | Research Support, Non-U.S. Gov't
Authors
Wade BO, Liu HW, Samora CP, Uhlmann F, Singleton MR
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