scholarly journals Strand Displacement by DNA Polymerase III Occurs through a τ-ψ-χ Link to Single-stranded DNA-binding Protein Coating the Lagging Strand Template

2009 ◽  
Vol 284 (46) ◽  
pp. 31672-31679 ◽  
Author(s):  
Quan Yuan ◽  
Charles S. McHenry
Keyword(s):  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Dna Polymerase Iii ◽  
Strand Displacement ◽  
Single Stranded Dna ◽  
Polymerase Iii ◽  
Protein Coating ◽  
Lagging Strand

scholarly journals Single-stranded DNA-binding Protein Recruits DNA Polymerase V to Primer Termini on RecA-coated DNA

2008 ◽  
Vol 283 (13) ◽  
pp. 8274-8282 ◽  
Author(s):  
Gali Arad ◽  
Ayal Hendel ◽  
Claus Urbanke ◽  
Ute Curth ◽  
Zvi Livneh
Keyword(s):  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Single Stranded Dna ◽  
Dna Polymerase V

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.

The role of gene A protein and E. coli rep protein in the replication of ɸX 174 replicative form DNA

1980 ◽  
Vol 210 (1180) ◽  
pp. 337-349 ◽  
Keyword(s):  
Dna Binding ◽  
Dna Polymerase ◽  
Binding Protein ◽  
Dna Binding Protein ◽  
Origin Of Replication ◽  
Electron Microscopic ◽  
Single Stranded Dna ◽  
Rep Protein ◽  
E Coli

The gene A protein of bacteriophage ɸX 174 initiates replication of super-twisted RFI DNA by cleaving the viral (+) strand at the origin of replication and binding to the 5' end. Upon addition of E. coli rep protein (single-stranded DNA dependent ATPase), E. coli single-stranded DNA binding protein and ATP, complete unwinding of the two strands occurs. Electron microscopic analyses of intermediates in the reaction reveal that the unwinding occurs by movement of the 5' end into the duplex, displacing the viral strand in the form of a single-stranded loop. Since unwinding will not occur in the absence of either gene A protein or rep protein, it is presumed that the rep protein interacts to form a complex with the bound gene A protein. Single-stranded DNA binding protein facilitates the unwinding by binding to the exposed single-stranded DNA. Further addition of the four deoxyribotriphosphates and DNA polymerase III holoenzyme to the reaction results in synthesis of viral (+) single-stranded circles in amounts exceeding that of the input template. A model describing the role of gene A protein and rep protein in duplex DNA replication is presented and other properties of gene A protein discussed.

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