| Autor: |
Marsilio, E, Cheng, S H, Schaffhausen, B, Paucha, E, Livingston, D M |
| Zdroj: |
The Journal of Virology; October 1991, Vol. 65 Issue: 10 p5647-5652, 6p |
| Abstrakt: |
Simian virus 40 large T antigen (T) can transform cultured cells, but the mechanisms by which it functions are not entirely understood. Several lines of evidence have suggested that the amino-terminal approximately 130 residues of T may be sufficient to confer the transforming capability. Oligonucleotide-directed mutagenesis was used to generate a series of deletion and substitution mutants within the amino-terminal 82 residues of T, the segment which is shared with simian virus 40 small t antigen (t). Results of stability and transformation assays of these mutants strongly suggest that the 1-to-82 region of T contains sequences which govern T transforming activity and affect in vivo stability. Instability and a defect in transforming activity could be separated from one another genetically. Thus, the 1-to-82 region appears to contain a specific region that contributes to the transforming function of the protein. This segment operates by means other than the simple binding of pRb and/or p107. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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