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TitleCryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 114, Issue 10, Page E1848-E1856, Year 2017
Publish dateMar 7, 2017
AuthorsArkadiusz W Kulczyk / Arne Moeller / Peter Meyer / Piotr Sliz / Charles C Richardson /
PubMed AbstractWe present a structure of the ∼650-kDa functional replisome of bacteriophage T7 assembled on DNA resembling a replication fork. A structure of the complex consisting of six domains of DNA helicase, ...We present a structure of the ∼650-kDa functional replisome of bacteriophage T7 assembled on DNA resembling a replication fork. A structure of the complex consisting of six domains of DNA helicase, five domains of RNA primase, two DNA polymerases, and two thioredoxin (processivity factor) molecules was determined by single-particle cryo-electron microscopy. The two molecules of DNA polymerase adopt a different spatial arrangement at the replication fork, reflecting their roles in leading- and lagging-strand synthesis. The structure, in combination with biochemical data, reveals molecular mechanisms for coordination of leading- and lagging-strand synthesis. Because mechanisms of DNA replication are highly conserved, the observations are relevant to other replication systems.
External linksProc Natl Acad Sci U S A / PubMed:28223502 / PubMed Central
MethodsEM (single particle)
Resolution13.8 Å
Structure data

EMDB-8565:
Cryo-EM structure of bacteriphage T7 replisome
Method: EM (single particle) / Resolution: 13.8 Å

Source
  • Enterobacteria phage T7 (virus)

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