Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis

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  • Arkadiusz W. Kulczyk, Harvard Medical School
  • ,
  • Arne Moeller
  • Peter Meyer, Harvard Medical School
  • ,
  • Piotr Sliz, Harvard Medical School
  • ,
  • Charles C. Richardson, Harvard Medical School

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.

TidsskriftProceedings of the National Academy of Sciences of the United States of America
Sider (fra-til)E1848-E1856
Antal sider9
StatusUdgivet - 7 mar. 2017

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