The Eukaryotic Replisome Goes Under the Microscope

Curr Biol. 2016 Mar 21;26(6):R247-56. doi: 10.1016/j.cub.2016.02.034.


The machinery at the eukaryotic replication fork has seen many new structural advances using electron microscopy and crystallography. Recent structures of eukaryotic replisome components include the Mcm2-7 complex, the CMG helicase, DNA polymerases, a Ctf4 trimer hub and the first look at a core replisome of 20 different proteins containing the helicase, primase, leading polymerase and a lagging strand polymerase. The eukaryotic core replisome shows an unanticipated architecture, with one polymerase sitting above the helicase and the other below. Additionally, structures of Mcm2 bound to an H3/H4 tetramer suggest a direct role of the replisome in handling nucleosomes, which are important to DNA organization and gene regulation. This review provides a summary of some of the many recent advances in the structure of the eukaryotic replisome.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Crystallography
  • DNA Helicases / chemistry
  • DNA Helicases / metabolism
  • DNA Replication*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • DNA-Directed DNA Polymerase / chemistry
  • DNA-Directed DNA Polymerase / metabolism*
  • Microscopy, Electron
  • Minichromosome Maintenance Proteins / chemistry*
  • Minichromosome Maintenance Proteins / metabolism
  • Nucleosomes / chemistry
  • Nucleosomes / metabolism
  • Saccharomyces cerevisiae Proteins / chemistry
  • Saccharomyces cerevisiae Proteins / metabolism


  • CTF4 protein, S cerevisiae
  • DNA-Binding Proteins
  • Nucleosomes
  • Saccharomyces cerevisiae Proteins
  • DNA-Directed DNA Polymerase
  • DNA Helicases
  • MCM2 protein, S cerevisiae
  • Minichromosome Maintenance Proteins