ArticleJournal of virology1996
An N-terminal deletion mutant of simian virus 40 (SV40) large T antigen oligomerizes incorrectly on SV40 DNA but retains the ability to bind to DNA polymerase alpha and replicate SV40 DNA in vitro.
Article in Journal of virology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- Polyomavirus large T antigen binds symmetrical repeats at the viral origin in an asymmetrical manner.Journal of virology · 2013Article
- Analysis of the costructure of the simian virus 40 T-antigen origin binding domain with site I reveals a correlation between GAGGC spacing and spiral assembly.Journal of virology · 2013Article
- A screen for modulators of large T antigen's ATPase activity uncovers novel inhibitors of Simian Virus 40 and BK virus replication.Antiviral research · 2012Article
- Asymmetric assembly of Merkel cell polyomavirus large T-antigen origin binding domains at the viral origin.Journal of molecular biology · 2011Article
- Inhibition of Simian Virus 40 replication by targeting the molecular chaperone function and ATPase activity of T antigen.Virus research · 2009Article
- SV40 DNA replication: from the A gene to a nanomachine.Virology · 2009Review
- Direct interaction between the N- and C-terminal portions of the herpes simplex virus type 1 origin binding protein UL9 implies the formation of a head-to-tail dimer.Journal of virology · 2007Article
- Quantitative analysis of the binding of simian virus 40 large T antigen to DNA.Journal of virology · 2007Article
- The crystal structure of the SV40 T-antigen origin binding domain in complex with DNA.PLoS biology · 2007Article
- Chaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Molecular and cellular biology · 2002Article
- T antigens of simian virus 40: molecular chaperones for viral replication and tumorigenesis.Microbiology and molecular biology reviews : MMBR · 2002Review
- Mutational analysis of simian virus 40 T-antigen primosome activities in viral DNA replication.Journal of virology · 2002Article
- Role of single-stranded DNA binding activity of T antigen in simian virus 40 DNA replication.Journal of virology · 2001Article
- Conformational changes in simian virus 40 rearranged regulatory regions: effects of the 21-base-pair promoters and their location.Journal of virology · 1999Article
- The replication protein A binding site in simian virus 40 (SV40) T antigen and its role in the initial steps of SV40 DNA replication.Journal of virology · 1998Article
- Polyomavirus T antigens: molecular chaperones for multiprotein complexes.Journal of virology · 1998Review
- Transient viral DNA replication and repression of viral transcription are supported by the C-terminal domain of the bovine papillomavirus type 1 E1 protein.Journal of virology · 1998Article
- Tiny T antigen: an autonomous polyomavirus T antigen amino-terminal domain.Journal of virology · 1997Article
- The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
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Authors and funding
7 authors.
Funding
Abstract
A peptide encompassing the N-terminal 82 amino acids of simian virus 40 (SV40) large T antigen was previously shown to bind to the large subunit of DNA polymerase alpha-primase (I. Dornreiter, A. Höss, A. K. Arthur, and E. Fanning, EMBO J. 9:3329-3336, 1990). We report here that a mutant T antigen, T83-708, lacking residues 2 to 82 retained the ability to bind to DNA polymerase alpha-primase, implying that it carries a second binding site for DNA polymerase alpha-primase. The mutant protein also retained ATPase, helicase, and SV40 origin DNA-binding activity. However, its SV40 DNA replication activity in vitro was reduced compared with that of wild-type protein. The reduction in replication activity was accompanied by a lower DNA-binding affinity to SV40 origin sequences and aberrant oligomerization on viral origin DNA. Thus, the first 82 residues of SV40 T antigen are not strictly required for its interaction with DNA polymerase alpha-primase or for DNA replication function but may play a role in correct hexamer assembly and efficient DNA binding at the origin.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.