Strauss M, Argani P, Mohr I J, Gluzman Y
J Virol. 1987 Oct;61(10):3326-30. doi: 10.1128/JVI.61.10.3326-3330.1987.
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.
对猿猴病毒40大T抗原的起源特异性DNA结合结构域进行了分析,发现其C端边界位于氨基酸259处或之前。这并不包括位于氨基酸302至320处的锌指结构基序(J.M.伯格,《科学》232:485 - 486,1986年)。有趣的是,266和272个氨基酸及更大的N端片段显示出显著降低的起源结合活性。此外,还比较了从细菌和哺乳动物来源纯化的截短蛋白的特异性DNA结合特性。来自哺乳动物细胞的截短T抗原比其细菌对应物更有效地结合特定DNA片段。这些结果表明翻译后修饰在调节大T抗原的DNA结合活性中起作用。