Structural studies of RFC C tf18 reveal a novel chromatin recruitment role for Dcc1
| Autor: | Martin R. Singleton, Hon Wing Liu, Benjamin O. Wade, Catarina P. Samora, Frank Uhlmann |
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| Rok vydání: | 2017 |
| Předmět: |
S‐phase checkpoint
Models Molecular 0301 basic medicine Saccharomyces cerevisiae Proteins Protein Conformation X‐ray crystallography Biology Biochemistry DNA-binding protein Article Structure-Activity Relationship 03 medical and health sciences chemistry.chemical_compound Replication factor C Structural Biology Genetics Protein Interaction Domains and Motifs Amino Acid Sequence Molecular Biology Dcc1 Cell Cycle Ctf18 DNA replication DNA Replication Repair & Recombination Articles Processivity Chromatin sister chromatid cohesion 3. Good health Cell biology DNA-Binding Proteins Establishment of sister chromatid cohesion 030104 developmental biology chemistry Origin recognition complex Protein Multimerization DNA Protein Binding |
| Zdroj: | EMBO Reports |
| ISSN: | 1469-3178 1469-221X |
| DOI: | 10.15252/embr.201642825 |
| Popis: | Replication factor C complexes load and unload processivity clamps from DNA and are involved in multiple DNA replication and repair pathways. The RFCC 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, RFCC 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. |
| Databáze: | OpenAIRE |
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