Ctf4 organizes sister replisomes and Pol α into a replication factory.
CMG helicase
Ctf4
DNA replication
S. cerevisiae
biochemistry
chemical biology
nucleosomes
replication factory
sister replication forks
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
07 10 2019
07 10 2019
Historique:
received:
04
04
2019
accepted:
04
10
2019
pubmed:
8
10
2019
medline:
12
3
2020
entrez:
8
10
2019
Statut:
epublish
Résumé
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
Identifiants
pubmed: 31589141
doi: 10.7554/eLife.47405
pii: 47405
pmc: PMC6800005
doi:
pii:
Substances chimiques
CTF4 protein, S cerevisiae
0
DNA, Fungal
0
DNA-Binding Proteins
0
Saccharomyces cerevisiae Proteins
0
DNA Polymerase I
EC 2.7.7.7
Banques de données
PDB
['6PTJ', '6PTN', '6PTO']
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM115809
Pays : United States
Organisme : NIH HHS
ID : GM115809
Pays : United States
Organisme : NIH HHS
ID : GM131754
Pays : United States
Informations de copyright
© 2019, Yuan et al.
Déclaration de conflit d'intérêts
ZY, RG, RS, DZ, LB, NY, GZ, MO, HL No competing interests declared
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