Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication Journal Article

   


Authors: Dean, F. B.; Bullock, P.; Murakami, Y.; Wobbe, C. R.; Weissbach, L.; Hurwitz, J.
Article Title: Simian virus 40 (SV40) DNA replication: SV40 large T antigen unwinds DNA containing the SV40 origin of replication
Abstract: The simian virus 40 (SV40) large T antigen (large tumor antigen), in conjunction with a topoisomerase, a DNA binding protein, and ATP, catalyzed the conversion of a circular duplex DNA molecule containing the SV40 origin of replication to a form with unusual electrophoretic mobility that we have named form U. Analysis of this molecule revealed it to be a highly underwound covalently closed circle. DNA unwinding was not detected with DNA containing a SV40 T-antigen binding site II mutation that renders the DNA inactive in replication. The unwinding reaction requires the action of a helicase, and SV40 T-antigen preparations contain such an activity. The T-antigen-associated ability to unwind DNA copurified with other activities intrinsic to T antigen [ability to support replication of SV40 DNA containing the SV40 origin, poly(dT)-stimulated ATPase activity, and DNA helicase]. However, in contrast to the unwinding activity, the SV40 T-antigen-associated helicase activity was not sequence-specific. A variety of labeled oligonucleotides hybridized with circular single-stranded DNA were displaced by T antigen in the presence of ATP.
Keywords: nonhuman; dna replication; hela cells; virus large t antigen; simian virus 40; plasmids; dna, viral; radioisotope; antigens, polyomavirus transforming; adenosine triphosphatases; electrophoresis; dna topoisomerases, type ii; dna topoisomerases, type i; antigens, viral, tumor; oncogene proteins, viral; simiae; circular dna; simian virus; humans; priority journal
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 84
Issue: 1
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1987-01-01
Start Page: 16
End Page: 20
Language: English
DOI: 10.1073/pnas.84.1.16
PUBMED: 3025851
PROVIDER: scopus
PMCID: PMC304132
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0009607249&doi=10.1073%2fpnas.84.1.16&partnerID=40&md5=bb1fbe8a241d7a1cd843f5903c7fd659
Notes: Article -- Export Date: 5 February 2021 -- Source: Scopus
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MSK Authors
  1. Jerard Hurwitz
    206 Hurwitz
  2. Frank B. Dean
    23 Dean
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