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Structural studies of RFC C tf18 reveal a novel chromatin recruitment role for Dcc1

DOI: 10.15252/embr.201642825 DOI Help

Authors: Benjamin O. Wade (The Francis Crick Institute (LIF)) , Hon Wing Liu (The Francis Crick Institute) , Catarina P. Samora (The Francis Crick Institute) , Frank Uhlmann (The Francis Crick Institute) , Martin R. Singleton (The Francis Crick Institute (LIF))
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Embo Reports

State: Published (Approved)
Published: February 2017
Diamond Proposal Number(s): 9826

Open Access Open Access

Abstract: Replication factor C complexes load and unload processivity clamps from DNA and are involved in multiple DNA replication and repair pathways. The RFCCtf18 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, RFCCtf18 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.

Journal Keywords: Ctf18; Dcc1; sister chromatid cohesion; S‐phase checkpoint; X‐ray crystallography

Subject Areas: Biology and Bio-materials

Instruments: I03-Macromolecular Crystallography

Added On: 14/02/2017 10:50


Discipline Tags:

Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)