ArticleNucleic acids research2002
Preformed hexamers of SV40 T antigen are active in RNA and origin-DNA unwinding.
Article in Nucleic acids research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Proteomics Analysis of the Polyomavirus DNA Replication Initiation Complex Reveals Novel Functional Phosphorylated Residues and Associated Proteins.International journal of molecular sciences · 2024Article
- SV40 T antigen interactions with ssDNA and replication protein A: a regulatory role of T antigen monomers in lagging strand DNA replication.Nucleic acids research · 2020Article
- Article
- Identification and functional characterization of regions that can be crosslinked to RNA in the helicase-like domain of BaMV replicase.Virology · 2009Article
- PCNA damage caused by antineoplastic drugs.Biochemical pharmacology · 2008Article
- Simian virus 40 DNA replication is dependent on an interaction between topoisomerase I and the C-terminal end of T antigen.Journal of virology · 2008Article
- Ddx42p--a human DEAD box protein with RNA chaperone activities.Nucleic acids research · 2006Article
- Two heads are better than one: regulation of DNA replication by hexameric helicases.Genes & development · 2004Review
- Interactions required for binding of simian virus 40 T antigen to the viral origin and molecular modeling of initial assembly events.Journal of virology · 2004Article
- Large T antigen on the simian virus 40 origin of replication: a 3D snapshot prior to DNA replication.The EMBO journal · 2003Article
- Nonspecific double-stranded DNA binding activity of simian virus 40 large T antigen is involved in melting and unwinding of the origin.Journal of virology · 2003Article
- The cap region of topoisomerase I binds to sites near both ends of simian virus 40 T antigen.Journal of virology · 2003Article
- Bidirectional DNA unwinding by a ternary complex of T antigen, nucleolin and topoisomerase I.EMBO reports · 2003Article
- Oligomerization and activity of the helicase domain of the tobacco mosaic virus 126- and 183-kilodalton replicase proteins.Journal of virology · 2003Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Preformed hexamers of simian virus 40 (SV40) large tumor antigen (T antigen) constitute the bulk of T antigen in infected cells and are stable under physiological conditions. In spite of this they could not be assigned a function in virus replication or transformation. We report that preformed hexamers represent the active T antigen RNA helicase. Monomers and smaller oligomeric forms of T antigen were inactive due to the lack of hexamer formation under RNA unwinding conditions. In contrast to the immunologically related cellular DEAD-box protein p68, the T antigen RNA helicase is found to act in a much more processive way and it does not catalyze rearrangements of structured RNAs. Thereby, it rather seems to resemble other virus-encoded RNA helicases, like vaccinia virus NPH-II. Surprisingly, in our hands preformed hexamers also strikingly bound to and unwound the SV40 replication origin, pointing to a possible role of preformed hexamers in the initiation step of viral DNA replication. Furthermore, we have detected an extra hexamer-specific, high-affinity T antigen ATP binding site with a very slow exchange rate constant, the function of which is discussed.
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