Abstract
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.
MeSH Terms
Amino Acid Sequence
Animals
Antigens, Polyomavirus Transforming/genetics
Cell Line
Cell Transformation, Viral
Chromosome Deletion
DNA Replication/drug effects
Molecular Sequence Data
Mutation
Plasmids
Simian virus 40/genetics,immunology
Theophylline/pharmacology
Transcriptional Activation
Chemicals
Antigens, Polyomavirus Transforming
Theophylline
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Jog P
Department of Microbiology and Immunology, Northwestern University Medical School, Chicago, Illinois 60611-3008.
Joshi B
Dhamankar V
Imperiale M J
Rutila J
Rundell K
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