5HOG

Crystal structure of the carboxy-terminal domain of yeast Ctf4 bound to Dna2.

Summary for 5HOG

• Entry DOI: 10.2210/pdb5hog/pdb
• Related: 4C8H 4C8S 4C93 4C95
• Descriptor: DNA polymerase alpha-binding protein, Dna2p (3 entities in total)
• Functional Keywords: dna replication, adaptor protein, beta-propeller domain, replication
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: Q01454
• Total number of polymer chains: 5
• Total formula weight: 167178.54

Authors

Simon, A.C.,Pellegrini, L. (deposition date: 2016-01-19, release date: 2016-06-22, Last modification date: 2024-05-08)

Primary citation

Villa, F.,Simon, A.C.,Ortiz Bazan, M.A.,Kilkenny, M.L.,Wirthensohn, D.,Wightman, M.,Matak-Vinkovic, D.,Pellegrini, L.,Labib, K.
Ctf4 Is a Hub in the Eukaryotic Replisome that Links Multiple CIP-Box Proteins to the CMG Helicase.
Mol.Cell, 63:385-396, 2016

PubMed Abstract: Replisome 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 α lagging-strand polymerase by the trimeric adaptor Ctf4. Here, we identify new Ctf4 partners in addition to Pol α 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.

PubMed: 27397685
DOI: 10.1016/j.molcel.2016.06.009

Experimental method

X-RAY DIFFRACTION (3.092 Å)