5hoi
Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Tof2.Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Tof2.
Structural highlights
FunctionCTF4_YEAST Accessory factor for DNA replication. It plays a role in accurately duplicating the genome in vivo. Publication Abstract from PubMedReplisome assembly at eukaryotic replication forks connects the DNA helicase to DNA polymerases and many other factors. The helicase binds the leading-strand polymerase directly, but is connected to the Pol alpha lagging-strand polymerase by the trimeric adaptor Ctf4. Here, we identify new Ctf4 partners in addition to Pol alpha and helicase, all of which contain a "Ctf4-interacting-peptide" or CIP-box. Crystallographic analysis classifies CIP-boxes into two related groups that target different sites on Ctf4. Mutations in the CIP-box motifs of the Dna2 nuclease or the rDNA-associated protein Tof2 do not perturb DNA synthesis genome-wide, but instead lead to a dramatic shortening of chromosome 12 that contains the large array of rDNA repeats. Our data reveal unexpected complexity of Ctf4 function, as a hub that connects multiple accessory factors to the replisome. Most strikingly, Ctf4-dependent recruitment of CIP-box proteins couples other processes to DNA synthesis, including rDNA copy-number regulation. Ctf4 Is a Hub in the Eukaryotic Replisome that Links Multiple CIP-Box Proteins to the CMG Helicase.,Villa F, Simon AC, Ortiz Bazan MA, Kilkenny ML, Wirthensohn D, Wightman M, Matak-Vinkovic D, Pellegrini L, Labib K Mol Cell. 2016 Jul 5. pii: S1097-2765(16)30240-4. doi:, 10.1016/j.molcel.2016.06.009. PMID:27397685[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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