Ewen M E, Ludlow J W, Marsilio E, DeCaprio J A, Millikan R C, Cheng S H, Paucha E, Livingston D M
Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
Cell. 1989 Jul 28;58(2):257-67. doi: 10.1016/0092-8674(89)90840-4.
In addition to Rb and p53, a third cellular protein, p120 in monkey and p118 in human cells, forms a specific complex with SV40 large T antigen (T). p118/120 is not a product of the Rb-gene. As was shown with T/Rb complex formation, the interaction between T and p120 is dependent on the intact nature of a ten residue, transformation-controlling domain in T (residues 105-114). In mouse cells, a readily detectable protein of 115 kd was detected, which, like murine Rb, also forms a stable complex with T. Like p118/120, p115 binding is also dependent on the intact nature of the 105-114 sequence. Given their similar size and T antigen binding sequence dependence, p115 and p118/120 may be products of the same gene in different species. These results suggest that interactions between T and p115/118/120, as well as T and Rb, contribute to the SV40 transforming mechanism.
除了Rb和p53外，第三种细胞蛋白（猴细胞中的p120和人细胞中的p118）与SV40大T抗原（T）形成特异性复合物。p118/120不是Rb基因的产物。正如T/Rb复合物形成所显示的那样，T与p120之间的相互作用取决于T中一个十肽转化控制结构域（第105 - 114位氨基酸残基）的完整性质。在小鼠细胞中，检测到一种易于检测的115kd蛋白质，它与鼠Rb一样，也与T形成稳定复合物。与p118/120一样，p115的结合也取决于105 - 114序列的完整性质。鉴于它们相似的大小和T抗原结合序列依赖性，p115和p118/120可能是不同物种中同一基因的产物。这些结果表明，T与p115/118/120之间以及T与Rb之间的相互作用有助于SV40的转化机制。
