The Eukaryotic Replisome Goes Under the Microscope

O'Donnell, Mike; Li, Huilin

doi:10.1016/j.cub.2016.02.034

Title: The Eukaryotic Replisome Goes Under the Microscope

Journal Article · Mon Mar 21 00:00:00 EDT 2016 · Current Biology

DOI:https://doi.org/10.1016/j.cub.2016.02.034· OSTI ID:1341599

O'Donnell, Mike ^[1]; Li, Huilin ^[2]

Rockefeller Univ., New York, NY (United States). DNA Replication Lab.; Howard Hughes Medical Inst., Chevy Chase, MD (United States)
Stony Brook Univ., NY (United States); Brookhaven National Lab. (BNL), Upton, NY (United States)

The machinery at the eukaryotic replication fork has seen many new structural advances using EM 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.

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Research Organization:: Brookhaven National Laboratory (BNL), Upton, NY (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER)

Grant/Contract Number:: SC00112704

OSTI ID:: 1341599

Report Number(s):: BNL-112356-2016-JA

Journal Information:: Current Biology, Vol. 26, Issue 6; ISSN 0960-9822

Publisher:: ElsevierCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 24 works

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