Mutational analysis of simian virus 40 small-t antigen.
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.
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Department of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois 60611-3008.
Joshi
B
B
Dhamankar
V
V
Imperiale
M J
MJ
Rutila
J
J
Rundell
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000235:genetics*; D002460:Cell Line; D002472:Cell Transformation, Viral; D002872:Chromosome Deletion; D004261:DNA Replication / Q000187:drug effects; D008969:Molecular Sequence Data; D009154:Mutation; D010957:Plasmids; D013539:Simian virus 40 / Q000235:genetics* / Q000276:immunology; D013806:Theophylline / Q000494:pharmacology; D015533:Transcriptional Activation
D000952:Antigens, Polyomavirus Transforming; D013806:Theophylline