The Eukaryotic Replisome Goes Under the Microscope

Mike O’Donnell

doi:10.1016/j.cub.2016.02.034

2016-03-01

Mike O’Donnell *

Huilin Li *

DOI：10.1016/j.cub.2016.02.034

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摘要

En 中文

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.

Keyword:

DNA-POLYMERASE-EPSILON

MINICHROMOSOME MAINTENANCE PROTEIN

REPLICATIVE HEXAMERIC HELICASE

SACCHAROMYCES-CEREVISIAE

STRUCTURAL BASIS

MCM2-7 HELICASE

POL ALPHA

CRYSTAL-STRUCTURE

III HOLOENZYME

FORK HELICASE

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期刊

Current Biology

IF:

7.5

论文数:

2.2W

被引数:

7.8W

机构

rockefeller university

学者数:

6.6K

论文数: 4.9K

被引数: 15

stony brook university

学者数:

1.4W

论文数: 1.0W

被引数: 20

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