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TitleCtf4 organizes sister replisomes and Pol α into a replication factory.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateOct 7, 2019
AuthorsZuanning Yuan / Roxana Georgescu / Ruda de Luna Almeida Santos / Daniel Zhang / Lin Bai / Nina Y Yao / Gongpu Zhao / Michael E O'Donnell / Huilin Li /
PubMed AbstractThe 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 ...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.
External linksElife / PubMed:31589141 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 12.0 Å
Structure data

20471

6ptj

EMDB-20471, PDB-6ptj:
Structure of Ctf4 trimer in complex with one CMG helicase
Method: EM (single particle) / Resolution: 3.8 Å

20472

6ptn

EMDB-20472, PDB-6ptn:
Structure of Ctf4 trimer in complex with two CMG helicases
Method: EM (single particle) / Resolution: 5.8 Å

20473

6pto

EMDB-20473, PDB-6pto:
Structure of Ctf4 trimer in complex with three CMG helicases
Method: EM (single particle) / Resolution: 7.0 Å

EMDB-20744:
Cryo-EM map of the S. cerevisiae primase-polymerase alpha bound to the Ctf4 trimer at 12 A resolution
Method: EM (single particle) / Resolution: 12.0 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsREPLICATION / Replication factory / sister replication forks / Ctf4/AND1 / DNA replication / CMG helicase / Cryo-EM / CMG-Ctf4

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