Abstract
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.
MeSH Terms
Animals
Antigens, Polyomavirus Transforming
Antigens, Viral, Tumor/analysis,genetics,metabolism
Bacterial Proteins/metabolism
DNA, Viral/metabolism
DNA-Binding Proteins/analysis
HeLa Cells
Humans
Oncogene Proteins, Viral/analysis,genetics,metabolism
Protein Processing, Post-Translational
Simian virus 40/genetics,immunology
Chemicals
Antigens, Polyomavirus Transforming
Antigens, Viral, Tumor
Bacterial Proteins
DNA, Viral
DNA-Binding Proteins
Oncogene Proteins, Viral
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Strauss M
Argani P
Mohr I J
Gluzman Y
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