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TitleCMG-Pol epsilon dynamics suggests a mechanism for the establishment of leading-strand synthesis in the eukaryotic replisome.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 16, Page 4141-4146, Year 2017
Publish dateApr 18, 2017
AuthorsJin Chuan Zhou / Agnieszka Janska / Panchali Goswami / Ludovic Renault / Ferdos Abid Ali / Abhay Kotecha / John F X Diffley / Alessandro Costa /
PubMed AbstractThe replisome unwinds and synthesizes DNA for genome duplication. In eukaryotes, the Cdc45-MCM-GINS (CMG) helicase and the leading-strand polymerase, Pol epsilon, form a stable assembly. The ...The replisome unwinds and synthesizes DNA for genome duplication. In eukaryotes, the Cdc45-MCM-GINS (CMG) helicase and the leading-strand polymerase, Pol epsilon, form a stable assembly. The mechanism for coupling DNA unwinding with synthesis is starting to be elucidated, however the architecture and dynamics of the replication fork remain only partially understood, preventing a molecular understanding of chromosome replication. To address this issue, we conducted a systematic single-particle EM study on multiple permutations of the reconstituted CMG-Pol epsilon assembly. Pol epsilon contains two flexibly tethered lobes. The noncatalytic lobe is anchored to the motor of the helicase, whereas the polymerization domain extends toward the side of the helicase. We observe two alternate configurations of the DNA synthesis domain in the CMG-bound Pol epsilon. We propose that this conformational switch might control DNA template engagement and release, modulating replisome progression.
External linksProc Natl Acad Sci U S A / PubMed:28373564 / PubMed Central
MethodsEM (single particle)
Resolution23.7 - 29.6 Å
Structure data

EMDB-3642:
Full-length complex of CMG helicase with polymerase epsilon
Method: EM (single particle) / Resolution: 24.4 Å

EMDB-3643:
Complex of CMG helicase with polymerase epsilon lacking the catalytic domain of Pol2
Method: EM (single particle) / Resolution: 29.6 Å

EMDB-3644:
Full-length CMG helicase complex
Method: EM (single particle) / Resolution: 23.7 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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