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Proc Natl Acad Sci U S A. 2017 Mar 7;114(10):E1848-E1856. doi: 10.1073/pnas.1701252114. Epub 2017 Feb 21.

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

Author information

1
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115; arek@hms.harvard.edu ccr@hms.harvard.edu.
2
Department of Molecular Biology and Genetics, The Danish Research Institute of Translational Neuroscience, Aarhus University, 8000 Aarhus, Denmark.
3
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.

Abstract

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.

KEYWORDS:

DNA polymerase; DNA replication; coordination of leading- and lagging-strands synthesis; cryo-EM structure; replisome

PMID:
28223502
PMCID:
PMC5347612
DOI:
10.1073/pnas.1701252114
[Indexed for MEDLINE]
Free PMC Article

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