scholarly journals The adenovirus DNA binding protein and adenovirus DNA polymerase interact to catalyze elongation of primed DNA templates.

1986 ◽  
Vol 261 (22) ◽  
pp. 10218-10227 ◽  
Author(s):  
J O Lindenbaum ◽  
J Field ◽  
J Hurwitz
2008 ◽  
Vol 283 (13) ◽  
pp. 8274-8282 ◽  
Author(s):  
Gali Arad ◽  
Ayal Hendel ◽  
Claus Urbanke ◽  
Ute Curth ◽  
Zvi Livneh

1993 ◽  
Vol 74 (6) ◽  
pp. 1003-1009 ◽  
Author(s):  
A. D. Agulnick ◽  
J. R. Thompson ◽  
S. Iyengar ◽  
G. Pearson ◽  
D. Ablashi ◽  
...  

2011 ◽  
Vol 286 (18) ◽  
pp. 15619-15624 ◽  
Author(s):  
Isabella Muylaert ◽  
Ka-Wei Tang ◽  
Per Elias

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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