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Science 19 June 1992:
Vol. 256. no. 5064, pp. 1656 - 1661
DOI: 10.1126/science.256.5064.1656
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Articles

Strand-Specific Recognition of a Synthetic DNA Replication Fork by the SV40 Large Tumor Antigen

Dhruba J. SenGupta and James A. Borowiec

The mechanism by which DNA helicases unwind DNA was tested; an "unwinding complex" between the SV40 large tumor antigen (T antigen) and a DNA molecule designed to resemble a replication fork was probed. In an adenosine triphosphate (ATP)—dependent reaction, T antigen quantitatively recognized this synthetic replication fork and bound the DNA primarily as a hexamer. The T antigen bound only one of the two strands at the fork, an asymmetric interaction consistent with the 3' rarr 5' directionality of the DNA helicase activity of T antigen. Binding to chemically modified DNA substrates indicated that the DNA helicase recognized the DNA primarily through the sugar-phosphate backbone. Ethylation of six top strand phosphates at the junction of single-stranded and double-stranded DNA inhibited the DNA helicase activity of T antigen. Neither a 3' single-stranded end on the DNA substrate nor ATP hydrolysis was required for T antigen to bind the replication fork. These data suggest that T antigen can directly bind the replication fork through recognition of a fork-specific structure.


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Common determinants in DNA melting and helicase-catalysed DNA unwinding by papillomavirus replication protein E1.
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The roles of the residues on the channel {beta}-hairpin and loop structures of simian virus 40 hexameric helicase.
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Interactions Required for Binding of Simian Virus 40 T Antigen to the Viral Origin and Molecular Modeling of Initial Assembly Events.
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J. Virol. 78, 2921-2934
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Nonspecific Double-Stranded DNA Binding Activity of Simian Virus 40 Large T Antigen Is Involved in Melting and Unwinding of the Origin.
J. Jiao and D. T. Simmons (2003)
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N. Tuteja (2003)
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Characterization of Simian Virus 40 T-antigen Double Hexamers Bound to a Replication Fork. THE ACTIVE FORM OF THE HELICASE.
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Mutational Analysis of Simian Virus 40 T-Antigen Primosome Activities in Viral DNA Replication.
R. D. Ott, Y. Wang, and E. Fanning (2002)
J. Virol. 76, 5121-5130
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Role of Single-Stranded DNA Binding Activity of T Antigen in Simian Virus 40 DNA Replication.
C. Wu, R. Roy, and D. T. Simmons (2001)
J. Virol. 75, 2839-2847
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Unwinding of nucleic acids by HCV NS3 helicase is sensitive to the structure of the duplex.
A. J. Tackett, L. Wei, C. E. Cameron, and K. D. Raney (2001)
Nucleic Acids Res. 29, 565-572
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The E1 Initiator Recognizes Multiple Overlapping Sites in the Papillomavirus Origin of DNA Replication.
G. Chen and A. Stenlund (2001)
J. Virol. 75, 292-302
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Sequence Requirements for the Assembly of Simian Virus 40 T Antigen and the T-Antigen Origin Binding Domain on the Viral Core Origin of Replication.
H. Y. Kim, B. A. Barbaro, W. S. Joo, A. E. Prack, K. R. Sreekumar, and P. A. Bullock (1999)
J. Virol. 73, 7543-7555
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The Origin DNA-Binding and Single-Stranded DNA-Binding Domains of Simian Virus 40 Large T Antigen Are Distinct.
C. Wu, D. Edgil, and D. T. Simmons (1998)
J. Virol. 72, 10256-10259
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Synthetic DNA Replication Bubbles Bound and Unwound with Twofold Symmetry by a Simian Virus 40 T-Antigen Double Hexamer.
N. V. Smelkova and J. A. Borowiec (1998)
J. Virol. 72, 8676-8681
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Does Single-stranded DNA Pass through the Inner Channel of the Protein Hexamer in the Complex with the Escherichia coli DnaB Helicase?. FLUORESCENCE ENERGY TRANSFER STUDIES.
M. J. Jezewska, S. Rajendran, D. Bujalowska, and W. Bujalowski (1998)
J. Biol. Chem. 273, 10515-10529
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