Wright P J, DeLucia A L, Tegtmeyer P
Mol Cell Biol. 1984 Dec;4(12):2631-8. doi: 10.1128/mcb.4.12.2631-2638.1984.
The simian virus 40 A protein (T antigen) recognized and bound to the consensus sequence 5'-GAGGC-3' in DNA from many sources. Sequence-specific binding to single pentanucleotides in randomly chosen DNA predominated over binding to nonspecific sequences. The asymmetric orientation of protein bound to nonorigin recognition sequences also resembled that of protein bound to the origin region of simian virus 40 DNA. Sequence variations in the DNA adjacent to single pentanucleotides influenced binding affinities even though methylation interference and protection studies did not reveal specific interactions outside of pentanucleotides. Thus, potential locations of A protein bound to any DNA can be predicted although the determinants of binding affinity are not yet understood. Sequence-specific binding of A protein to cellular DNA would provide a mechanism for specific alterations of host gene expression that facilitate viral function.
猿猴病毒40 A蛋白（T抗原）可识别并结合多种来源DNA中的共有序列5'-GAGGC-3'。在随机选择的DNA中，与单个五核苷酸的序列特异性结合比与非特异性序列的结合更为显著。与非起始识别序列结合的蛋白质的不对称取向也类似于与猿猴病毒40 DNA起始区域结合的蛋白质的取向。即使甲基化干扰和保护研究未揭示五核苷酸以外的特异性相互作用，但与单个五核苷酸相邻的DNA中的序列变异仍会影响结合亲和力。因此，尽管尚未了解结合亲和力的决定因素，但仍可预测A蛋白与任何DNA结合的潜在位置。A蛋白与细胞DNA的序列特异性结合将为宿主基因表达的特异性改变提供一种机制，从而促进病毒功能。
