Allosteric control of simian virus 40 T-antigen binding to viral origin DNA
- 1 June 1986
- journal article
- research article
- Published by American Society for Microbiology in Journal of Virology
- Vol. 58 (3) , 765-772
- https://doi.org/10.1128/jvi.58.3.765-772.1986
Abstract
Simian virus 40 (SV40) large tumor antigen (T antigen) possesses several biochemical activities localized in different domains of the protein. These activities include sequence-specific binding to two major sites, I and II, in the SV40 control region, ATPase, and nucleotide-binding activity. In the present communication, we present evidence that specific binding of immunopurified T antigen to SV40 DNA is markedly inhibited by low concentrations of ATP, dATP, GTP, and dGTP. The inhibition is reversible after removal of the nucleotide, suggesting that simple nucleotide binding rather than a covalent modification of T antigen in the presence of ATP is responsible for the inhibition. The results suggest that T antigen may assume two conformations, one active and one inactive in binding to the SV40 origin of replication. In the presence of purine nucleoside triphosphates, the inactive conformation is favored.This publication has 55 references indexed in Scilit:
- ATP-dependent specific binding of Tn3 transposase to Tn3 inverted repeatsNature, 1985
- Essential contact residues within SV40 large T antigen binding sites I and II identified by alkylation-interferenceCell, 1984
- Regulatory mutants of simian virus 40Journal of Molecular Biology, 1982
- T antigen repression of SV40 early transcription from two promotersCell, 1981
- Heavy metal intensification of DAB-based HRP reaction product.Journal of Histochemistry & Cytochemistry, 1981
- Cold-sensitive regulatory mutants of simian virus 40Journal of Molecular Biology, 1980
- Trans-complementable copy-number mutants of plasmid ColE1Nature, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Isolation of pure IgG1, IgG2a and IgG2b immunoglobulins from mouse serum using protein A-SepharoseImmunochemistry, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970