| Literature DB >> 21362621 |
Isabella Muylaert1, Ka-Wei Tang, Per Elias.
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.Mesh:
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Year: 2011 PMID: 21362621 PMCID: PMC3091170 DOI: 10.1074/jbc.R111.233981
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157