ATP-dependent formation of a specialized nucleoprotein structure by simian virus 40 (SV40) large tumor antigen at the SV40 replication origin Journal Article

   


Authors: Dean, F. B.; Dodson, M.; Echols, H.; Hurwitz, J.
Article Title: ATP-dependent formation of a specialized nucleoprotein structure by simian virus 40 (SV40) large tumor antigen at the SV40 replication origin
Abstract: The large tumor antigen (T antigen) specified by simian virus 40 (SV40) is required for viral DNA replication. To carry out its function, T antigen binds to duplex DNA at the origin of replication (oriSV40) and exerts a helicase activity that unwinds the two DNA strands. Previous work has defined two binding sites for T antigen near oriSV40, designated sites I and II; site II is within the 64-base-pair core sequence absolutely required for viral DNA replication. We have used electron microscopy and gel electrophoresis to characterize the interaction of T antigen with the origin region. We have found that effective binding to site II under conditions that support DNA replication requires ATP or a nonhydrolyzable analog. In the absence of ATP, T antigen binds mainly to site I; in the presence of ATP, both sites I and II are occupied, and binding is markedly increased. The ATP-dependent reaction generates a complex multimeric structure for T antigen. We conclude that T antigen forms an ATP-dependent nucleoprotein structure at oriSV40. We suggest that this nucleoprotein complex provides for the precise initiation of SV40 DNA replication.
Keywords: dna binding protein; genetics; dna-binding proteins; methodology; dna replication; electron microscopy; metabolism; microscopy, electron; simian virus 40; binding site; dna, viral; binding sites; virus replication; adenosine triphosphate; virus t antigen; polyacrylamide gel electrophoresis; electrophoresis, polyacrylamide gel; virus dna; antigens, viral, tumor; nucleoprotein; nucleoproteins; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 84
Issue: 24
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 1987-12-01
Start Page: 8981
End Page: 8985
Language: English
DOI: 10.1073/pnas.84.24.8981
PUBMED: 2827164
PROVIDER: scopus
PMCID: PMC299675
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0023474687&doi=10.1073%2fpnas.84.24.8981&partnerID=40&md5=d96a0cdfa4205a09d9303af87ee27372
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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