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

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaperJournal articleResearchpeer-review

DOI

  • 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.

Original languageEnglish
JournalProceedings of the National Academy of Sciences of the United States of America
Volume114
Issue10
Pages (from-to)E1848-E1856
Number of pages9
ISSN0027-8424
DOIs
Publication statusPublished - 7 Mar 2017

    Research areas

  • Coordination of leading- and lagging-strands synthesis, Cryo-EM structure, DNA polymerase, DNA replication, Replisome

See relations at Aarhus University Citationformats

ID: 117565862