Mutational analysis of simian virus 40 small-t antigen.
AUTOR(ES)
Jog, P
RESUMO
Several point mutations in the simian virus 40 (SV40) small-t antigen have been analyzed for their effects on protein stability, transformation, transactivation, and binding of two cellular proteins. All mutations which affected cysteine residues in two cysteine clusters produced highly unstable small-t antigens. Four point mutations outside these clusters and one in-frame deletion mutant, dl890, produced stable proteins but reduced transformation efficiency. These were able to transactivate the EII promoter and bind the cellular proteins, suggesting that these activities are not sufficient for small-t-mediated enhancement of transformation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=249472Documentos Relacionados
- Control of protein phosphatase 2A by simian virus 40 small-t antigen.
- Simian virus 40 small-t antigen binds two zinc ions.
- Presence in growth-arrested cells of cellular proteins that interact with simian virus 40 small-t antigen.
- Nucleotide sequence of the simian virus 40 small-t gene
- Dephosphorylation of simian virus 40 large-T antigen and p53 protein by protein phosphatase 2A: inhibition by small-t antigen.
