HeLa cell single-stranded DNA-binding protein increases the accuracy of DNA synthesis by DNA polymerase α in vitro

1992 ◽  
Vol 274 (1) ◽  
pp. 29-43 ◽  
Author(s):  
Michael P. Carty ◽  
Arthur S. Levine ◽  
Kathleen Dixon
2008 ◽  
Vol 283 (13) ◽  
pp. 8274-8282 ◽  
Author(s):  
Gali Arad ◽  
Ayal Hendel ◽  
Claus Urbanke ◽  
Ute Curth ◽  
Zvi Livneh

FEBS Letters ◽  
1988 ◽  
Vol 239 (2) ◽  
pp. 251-254 ◽  
Author(s):  
Hans L. Vos ◽  
Frédérique M. van der Lee ◽  
John S. Sussenbach

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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