Structural highlights
Function
G0S825_CHATD
Publication Abstract from PubMed
The Tof1-Csm3 fork protection complex has a central role in the replisome-it promotes the progression of DNA replication forks and protects them when they stall, while also enabling cohesion establishment and checkpoint responses. Here, I present the crystal structure of the Tof1-Csm3 complex from Chaetomium thermophilum at 3.1 A resolution. The structure reveals that both proteins together form an extended alpha helical repeat structure, which suggests a mechanical or scaffolding role for the complex. Expanding on this idea, I characterize a DNA interacting region and a cancer-associated Mrc1 binding site. This study provides the molecular basis for understanding the functions of the Tof1-Csm3 complex, its human orthologue the Timeless-Tipin complex and additionally the Drosophila circadian rhythm protein Timeless.
Crystal structure and interactions of the Tof1-Csm3 (Timeless-Tipin) fork protection complex.,Grabarczyk DB Nucleic Acids Res. 2020 May 29. pii: 5848492. doi: 10.1093/nar/gkaa456. PMID:32469068[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Grabarczyk DB. Crystal structure and interactions of the Tof1-Csm3 (Timeless-Tipin) fork protection complex. Nucleic Acids Res. 2020 May 29. pii: 5848492. doi: 10.1093/nar/gkaa456. PMID:32469068 doi:http://dx.doi.org/10.1093/nar/gkaa456
