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.
journal_name
J Viroljournal_title
Journal of virologyauthors
Kumar A,Meinke G,Reese DK,Moine S,Phelan PJ,Fradet-Turcotte A,Archambault J,Bohm A,Bullock PAdoi
10.1128/JVI.02451-06subject
Has Abstractpub_date
2007-05-01 00:00:00pages
4808-18issue
9eissn
0022-538Xissn
1098-5514pii
JVI.02451-06journal_volume
81pub_type
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