Publication: Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis
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2017
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National Academy of Sciences
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Kulczyk, Arkadiusz W., Arne Moeller, Peter Meyer, Piotr Sliz, and Charles C. Richardson. 2017. “Cryo-EM Structure of the Replisome Reveals Multiple Interactions Coordinating DNA Synthesis.” Proceedings of the National Academy of Sciences 114 (10): E1848–56. https://doi.org/10.1073/pnas.1701252114.
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Abstract
We present a structure of the similar to 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.
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