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

The Eukaryotic Replisome Goes Under the Microscope.

Author information

1
DNA Replication Lab, The Rockefeller University, 1230 York Avenue, New York, New York, USA; Howard Hughes Medical Institute. Electronic address: odonnel@rockefeller.edu.
2
Department of Biochemistry & Cell Biology, Stony Brook University, Stony Brook, New York, USA; Biology Department, Brookhaven National Laboratory, Upton, New York, USA. Electronic address: hli@bnl.gov.

Abstract

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.

PMID:
27003891
PMCID:
PMC4859309
DOI:
10.1016/j.cub.2016.02.034
[Indexed for MEDLINE]
Free PMC Article

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