Studies on the origin-specific DNA-binding domain of simian virus 40 large T antigen.
The origin-specific DNA-binding domain of simian virus 40 large T antigen was analyzed, and its C-terminal boundary was found to be at or before amino acid 259. This does not include the zinc finger structural motif located at amino acids 302 to 320 (J. M. Berg, Science 232:485-486, 1986). Interestingly, N-terminal fragments of 266 and 272 amino acids and larger displayed dramatically reduced origin-binding activity. In addition, the specific DNA-binding properties of truncated proteins purified from both bacterial and mammalian sources were compared. Truncated T antigens from mammalian cells bound specific DNA fragments more efficiently than did their bacterial counterparts. These results implicate posttranslational modification with a role in regulating the DNA-binding activity of large T antigen.
D000818:Animals; D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D004279:DNA, Viral / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000032:analysis*; D006367:HeLa Cells; D006801:Humans; D009856:Oncogene Proteins, Viral / Q000032:analysis* / Q000235:genetics / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D013539:Simian virus 40 / Q000235:genetics / Q000276:immunology*
D000952:Antigens, Polyomavirus Transforming; D000957:Antigens, Viral, Tumor; D001426:Bacterial Proteins; D004279:DNA, Viral; D004268:DNA-Binding Proteins; D009856:Oncogene Proteins, Viral