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Journal of Virology, September 2000, p. 8589-8600, Vol. 74, No. 18
Department of Biochemistry, Tufts University
School of Medicine, Boston, Massachusetts 02111
Received 10 April 2000/Accepted 14 June 2000
Using subfragments of the simian virus 40 (SV40) core origin, we
demonstrate that two alternative modules exist for the assembly of
T-antigen (T-ag) double hexamers. Pentanucleotides 1 and 3 and the
early palindrome (EP) constitute one assembly unit, while pentanucleotides 2 and 4 and the AT-rich region constitute a second, relatively weak, assembly unit. Related studies indicate that on the
unit made up of pentanucleotide 1 and 3 and the EP assembly unit, the
first hexamer forms on pentanucleotide 1 and that owing to additional
protein-DNA and protein-protein interactions, the second hexamer is
able to form on pentanucleotide 3. Oligomerization on the unit made up
of pentanucleotide 2 and 4 and the AT-rich region is initiated by
assembly of a hexamer on pentanucleotide 4; subsequent formation of the
second hexamer takes place on pentanucleotide 2. Given that
oligomerization on the SV40 origin is limited to double-hexamer
formation, it is likely that only a single module is used for the
initial assembly of T-ag double hexamers. Finally, we discuss the
evidence that nucleotide hydrolysis is required for the remodeling
events that result in the utilization of the second assembly unit.
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
The Simian Virus 40 Core Origin Contains Two Separate Sequence
Modules That Support T-Antigen Double-Hexamer Assembly

*
Corresponding author. Mailing address: Department of
Biochemistry A703, Tufts University School of Medicine, 136 Harrison Ave., Boston, MA 02111. Phone: (617) 636-0447. Fax: (617) 636-2409. E-mail: PBULLOCK{at}OPAL.TUFTS.EDU.
Present address: National Center for Biotechnology Information,
National Institutes of Health, Bethesda, MD 20894.
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