scholarly journals Dual Functions of Single-stranded DNA-binding Protein in Helicase Loading at the Bacteriophage T4 DNA Replication Fork

2004 ◽  
Vol 279 (18) ◽  
pp. 19035-19045 ◽  
Author(s):  
Yujie Ma ◽  
Tongsheng Wang ◽  
Jana L. Villemain ◽  
David P. Giedroc ◽  
Scott W. Morrical
Keyword(s):  
Dna Replication ◽  
Dna Binding ◽  
Replication Fork ◽  
Binding Protein ◽  
Bacteriophage T4 ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Helicase Loading ◽  
Dual Functions

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.

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