scholarly journals Virion-Associated Cofactor High-Mobility Group DNA-Binding Protein-1 Facilitates Transposition from the Herpes Simplex Virus/Sleeping BeautyAmplicon Vector Platform

2010 ◽  
Vol 21 (11) ◽  
pp. 1615-1622 ◽  
Author(s):  
Suresh de Silva ◽  
Louis T. Lotta ◽  
Clark A. Burris ◽  
William J. Bowers
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Binding Protein ◽  
High Mobility ◽  
Dna Binding Protein ◽  
High Mobility Group ◽  
Simplex Virus

scholarly journals Targeting Holliday junctions by origin DNA-binding protein of herpes simplex virus type 1

2016 ◽  
Vol 35 (4) ◽  
pp. 704-723 ◽  
Author(s):  
E.D. Moiseeva ◽  
N.P. Bazhulina ◽  
Y.G. Gursky ◽  
S.L. Grokhovsky ◽  
A.N. Surovaya ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Holliday Junctions ◽  
Simplex Virus

scholarly journals Replication and Recombination of Herpes Simplex Virus DNA

2011 ◽  
Vol 286 (18) ◽  
pp. 15619-15624 ◽  
Author(s):  
Isabella Muylaert ◽  
Ka-Wei Tang ◽  
Per Elias
Keyword(s):  
Herpes Simplex Virus ◽  
Dna Replication ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Cellular Proteins ◽  
Single Stranded Dna ◽  
Simplex Virus

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.

scholarly journals Herpes Simplex Virus Type 1 Single-Strand DNA Binding Protein ICP8 Enhances the Nuclease Activity of the UL12 Alkaline Nuclease by Increasing Its Processivity

2005 ◽  
Vol 79 (14) ◽  
pp. 9356-9358 ◽  
Author(s):  
Nina Bacher Reuven ◽  
Sandra K. Weller
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Herpes Simplex Virus Type ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Strand Exchange ◽  
Double Stranded Dna ◽  
Simplex Virus

ABSTRACT UL12 is a 5′- to 3′-exonuclease encoded by herpes simplex virus type 1 (HSV-1) which degrades single- and double-stranded DNA. UL12 and the single-strand DNA binding protein ICP8 mediate a strand exchange reaction. We found that ICP8 inhibited UL12 digestion of single-stranded DNA but stimulated digestion of double-stranded DNA threefold. The stimulatory effect of ICP8 was independent of a strand exchange reaction; furthermore, the effect was specific to ICP8, as it could not be reproduced by Escherichia coli single-stranded DNA binding protein. The effect of ICP8 on the rate of UL12 double-stranded DNA digestion is attributable to an increase in processivity in the presence of ICP8.

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