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Title: The Eukaryotic Replisome Goes Under the Microscope

Abstract

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.

Authors:
 [1];  [2]
  1. Rockefeller Univ., New York, NY (United States). DNA Replication Lab.; Howard Hughes Medical Inst., Chevy Chase, MD (United States)
  2. Stony Brook Univ., NY (United States); Brookhaven National Lab. (BNL), Upton, NY (United States)
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
OSTI Identifier:
1341599
Report Number(s):
BNL-112356-2016-JA
Journal ID: ISSN 0960-9822
Grant/Contract Number:  
SC00112704
Resource Type:
Accepted Manuscript
Journal Name:
Current Biology
Additional Journal Information:
Journal Volume: 26; Journal Issue: 6; Journal ID: ISSN 0960-9822
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; Electron Microscopy; Replisome; CMG; Helicase; DNA polymerase; Primase

Citation Formats

O'Donnell, Mike, and Li, Huilin. The Eukaryotic Replisome Goes Under the Microscope. United States: N. p., 2016. Web. doi:10.1016/j.cub.2016.02.034.
O'Donnell, Mike, & Li, Huilin. The Eukaryotic Replisome Goes Under the Microscope. United States. doi:10.1016/j.cub.2016.02.034.
O'Donnell, Mike, and Li, Huilin. Mon . "The Eukaryotic Replisome Goes Under the Microscope". United States. doi:10.1016/j.cub.2016.02.034. https://www.osti.gov/servlets/purl/1341599.
@article{osti_1341599,
title = {The Eukaryotic Replisome Goes Under the Microscope},
author = {O'Donnell, Mike and Li, Huilin},
abstractNote = {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.},
doi = {10.1016/j.cub.2016.02.034},
journal = {Current Biology},
number = 6,
volume = 26,
place = {United States},
year = {2016},
month = {3}
}

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Works referencing / citing this record:

The human CTF4-orthologue AND-1 interacts with DNA polymerase α/primase via its unique C-terminal HMG box
journal, November 2017

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