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- W2167096616 endingPage "4818" @default.
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- W2167096616 abstract "The interaction of simian virus 40 (SV40) T antigen (T-ag) with the viral origin has served as a model for studies of site-specific recognition of a eukaryotic replication origin and the mechanism of DNA unwinding. These studies have revealed that a motif termed the beta-hairpin is necessary for assembly of T-ag on the SV40 origin. Herein it is demonstrated that residues at the tip of the beta-hairpin are needed to melt the origin-flanking regions and that the T-ag helicase domain selectively assembles around one of the newly generated single strands in a manner that accounts for its 3'-to-5' helicase activity. Furthermore, T-ags mutated at the tip of the beta-hairpin are defective for oligomerization on duplex DNA; however, they can assemble on hybrid duplex DNA or single-stranded DNA (ssDNA) substrates provided the strand containing the 3' extension is present. Collectively, these experiments indicate that residues at the tip of the beta-hairpin generate ssDNA in the core origin and that the ssDNA is essential for subsequent oligomerization events." @default.
- W2167096616 created "2016-06-24" @default.
- W2167096616 creator A5001615594 @default.
- W2167096616 creator A5001943601 @default.
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- W2167096616 creator A5059223946 @default.
- W2167096616 creator A5071093993 @default.
- W2167096616 date "2007-05-01" @default.
- W2167096616 modified "2023-09-27" @default.
- W2167096616 title "Model for T-Antigen-Dependent Melting of the Simian Virus 40 Core Origin Based on Studies of the Interaction of the Beta-Hairpin with DNA" @default.
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