A region of SV40 large T antigen can substitute for a transforming domain of the adenovirus E1A products.
SV40 large T antigen contains a small region of amino acid sequence, conserved among the papovaviruses, that shows considerable similarity to conserved domain 2 of the adenovirus E1A oncogene, a domain which plays an important role in the E1A transforming functions. To learn whether the analogous SV40 T antigen sequences could substitute functionally for E1A domain 2, a chimaeric gene was constructed, coding for T antigen amino acid residues 101 to 118 in place of E1A domain 2. The resulting product showed much of the activity of the wild-type E1A products. It induced proliferation of primary BRK cells and cooperated with the ras oncogene to transform these cells fully. In addition, the chimaeric protein coprecipitated two cellular proteins whose specific binding to the E1A products depends on the presence of domain 2. The activity of the chimaeric product suggests that a similar functional unit exists in the transforming proteins of both SV40 and adenovirus, and that these proteins may exert their cell growth regulating effects through similar mechanisms.
Moran
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Cold Spring Harbor Laboratory, New York 11724.
D017456:Adenovirus Early Proteins; D000595:Amino Acid Sequence; D000818:Animals; D000952:Antigens, Polyomavirus Transforming / Q000502:physiology*; D002478:Cells, Cultured; D005818:Genetic Engineering; D006367:HeLa Cells; D006801:Humans; D007158:Immunologic Techniques; D008940:Mitotic Index; D008969:Molecular Sequence Data; D009856:Oncogene Proteins, Viral / Q000502:physiology*; D051381:Rats; D013329:Structure-Activity Relationship
D017456:Adenovirus Early Proteins; D000952:Antigens, Polyomavirus Transforming; D009856:Oncogene Proteins, Viral