例如:"lncRNA", "apoptosis", "WRKY"

Ctf4 organizes sister replisomes and Pol α into a replication factory.

Elife. 2019 Oct 07;8
Zuanning Yuan 1 , Roxana Georgescu 2 , Ruda de Luna Almeida Santos 1 , Daniel Zhang 2 , Lin Bai 1 , Nina Y Yao 2 , Gongpu Zhao 3 , Michael E O'Donnell 2 , Huilin Li 1
Zuanning Yuan 1 , Roxana Georgescu 2 , Ruda de Luna Almeida Santos 1 , Daniel Zhang 2 , Lin Bai 1 , Nina Y Yao 2 , Gongpu Zhao 3 , Michael E O'Donnell 2 , Huilin Li 1
+ et al

[No authors listed]

Author information
  • 1 Structural Biology Program, Van Andel Institute, Grand Rapids, United States.
  • 2 DNA Replication Laboratory, The Rockefeller University, New York, United States.
  • 3 David Van Andel Advanced Cryo-EM Suite, Van Andel Institute, Grand Rapids, United States.

摘要


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-Ctf43-1Pol 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.

KEYWORDS: CMG helicase, Ctf4, DNA replication, S. cerevisiae, biochemistry, chemical biology, nucleosomes, replication factory, sister replication forks