6PTJ

Structure of Ctf4 trimer in complex with one CMG helicase

Summary for 6PTJ

• Entry DOI: 10.2210/pdb6ptj/pdb
• EMDB information: 20471
• Descriptor: DNA replication complex GINS protein PSF1, DNA replication licensing factor MCM6, DNA replication licensing factor MCM7, ... (12 entities in total)
• Functional Keywords: replication factory, sister replication forks, ctf4/and1, dna replication, cmg helicase, replication
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 14
• Total formula weight: 1099612.39

Authors

Yuan, Z.,Georgescu, R.,Bai, L.,Santos, R.,Donnell, M.,Li, H. (deposition date: 2019-07-15, release date: 2019-11-20, Last modification date: 2024-10-30)

Primary citation

Yuan, Z.,Georgescu, R.,Santos, R.L.A.,Zhang, D.,Bai, L.,Yao, N.Y.,Zhao, G.,O'Donnell, M.E.,Li, H.
Ctf4 organizes sister replisomes and Pol alpha into a replication factory.
Elife, 8:-, 2019

PubMed Abstract: The current view is that eukaryotic replisomes are independent. Here we show that Ctf4 tightly dimerizes CMG helicase, with an extensive interface involving Psf2, Cdc45, and Sld5. Interestingly, Ctf4 binds only one Pol α-primase. Thus, Ctf4 may have evolved as a trimer to organize two helicases and one Pol α-primase into a replication factory. In the 2CMG-Ctf4-1Pol α-primase factory model, the two CMGs nearly face each other, placing the two lagging strands toward the center and two leading strands out the sides. The single Pol α-primase is centrally located and may prime both sister replisomes. The Ctf4-coupled-sister replisome model is consistent with cellular microscopy studies revealing two sister forks of an origin remain attached and are pushed forward from a protein platform. The replication factory model may facilitate parental nucleosome transfer during replication.

PubMed: 31589141
DOI: 10.7554/eLife.47405

Experimental method

ELECTRON MICROSCOPY (3.8 Å)