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Review
. 2011 May 6;286(18):15619-24.
doi: 10.1074/jbc.R111.233981. Epub 2011 Mar 1.

Replication and recombination of herpes simplex virus DNA

Isabella Muylaert  1 , Ka-Wei Tang, Per Elias
Affiliations
Review

Replication and recombination of herpes simplex virus DNA

Isabella Muylaert et al. J Biol Chem. .

Abstract

Replication of herpes simplex virus takes place in the cell nucleus and is carried out by a replisome composed of six viral proteins: the UL30-UL42 DNA polymerase, the UL5-UL8-UL52 helicase-primase, and the UL29 single-stranded DNA-binding protein ICP8. The replisome is loaded on origins of replication by the UL9 initiator origin-binding protein. Virus replication is intimately coupled to recombination and repair, often performed by cellular proteins. Here, we review new significant developments: the three-dimensional structures for the DNA polymerase, the polymerase accessory factor, and the single-stranded DNA-binding protein; the reconstitution of a functional replisome in vitro; the elucidation of the mechanism for activation of origins of DNA replication; the identification of cellular proteins actively involved in or responding to viral DNA replication; and the elucidation of requirements for formation of replication foci in the nucleus and effects on protein localization.

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Figures

FIGURE 1.
FIGURE 1.
Herpes simplex virus DNA replication. Upper, the linear genome is circularized by DNA ligase IV/XRCC4 and serves as template for the viral replication machinery. A first phase of theta-type replication, initiated at three redundant origins of replication oriS and oriL, is followed by rolling circle replication. Note that frequent recombination events generate molecules with a more complex structure (see text). The figure is adapted from Ref. . UL and US, unique long and short segments, respectively. Middle, the HSV-1 replication fork. Lower, HSV-1 replication causes a series of structural changes in the cell nucleus characterized by co-localization of replication, repair, and recombination proteins (for further details, see Ref. 18).
FIGURE 2.
FIGURE 2.
HSV-1 origins of replication activated by OBP and ICP8 in the presence of ATP. A dimer of OBP binds to a hairpin with helicase domains covering 3′-ssDNA and delivers ICP8 to ssDNA (26).
FIGURE 3.
FIGURE 3.
Structure of HSV-1 replication proteins. Shown are the UL30 DNA polymerase (31), the UL42 processivity factor with a C-terminal peptide from UL30 DNA polymerase (42), and a filament composed of ICP8 and ssDNA (65).
See this image and copyright information in PMC

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