scholarly journals Physical interaction between the herpes simplex virus 1 origin-binding protein and single-stranded DNA-binding protein ICP8.

1993 ◽  
Vol 90 (18) ◽  
pp. 8444-8448 ◽  
Author(s):  
P. E. Boehmer ◽  
I. R. Lehman
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Physical Interaction ◽  
Herpes Simplex Virus 1 ◽  
Single Stranded Dna ◽  
Origin Binding Protein ◽  
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 Identification of a Region of the Herpes Simplex Virus Single-Stranded DNA-Binding Protein Involved in Cooperative Binding

1998 ◽  
Vol 72 (1) ◽  
pp. 257-265 ◽  
Author(s):  
Kathleen C. Dudas ◽  
William T. Ruyechan
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Dna Binding ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Peptide Sequencing ◽  
Cooperative Binding ◽  
Single Stranded Dna ◽  
Shift Analysis ◽  
Simplex Virus

ABSTRACT We have identified a region of the herpes simplex virus major DNA-binding protein (ICP8) which is involved in cooperative binding to single-stranded DNA. This has been accomplished by analysis of ICP8 which was covalently modified by reaction with the extrinsic fluorophore fluorescein-5-maleimide (FM). Reaction conditions which result in the incorporation of 1 mol of FM per mol of ICP8 have been established. The binding properties of the modified protein were analyzed by polyacrylamide gel shift analysis with model oligonucleotides. This analysis indicates that while intrinsic binding is similar to that observed with unmodified protein, the cooperative binding of the modified protein to single-stranded DNA is significantly altered. Helix-destabilizing assays, whose results are a reflection of cooperative binding, also indicate that this property of ICP8 is decreased upon modification with FM. Mapping of the site of modification by cyanogen bromide cleavage and peptide sequencing has shown that the major site of modification is cysteine 254. This position in the primary structure of ICP8 is distinct from the regions previously shown to be involved in the interaction of this protein with single-stranded DNA.

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