Kaelin W G, Ewen M E, Livingston D M
Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
Mol Cell Biol. 1990 Jul;10(7):3761-9. doi: 10.1128/mcb.10.7.3761-3769.1990.
It has previously been demonstrated that the simian virus 40 large T antigen and adenovirus E1A proteins can form complexes with the retinoblastoma susceptibility gene product (RB). We studied the ability of these proteins to bind to mutant RB proteins in vitro. A region of RB spanning residues 379 to 792 was found to be both necessary and sufficient for binding to T or E1A. Furthermore, this region of RB contains sufficient structural information to mimic wild-type RB in its ability to distinguish between wild-type T and the transformation-defective T mutant K1. The results of competition experiments with peptide analogs of the RB-binding sequence in T suggest that this region of RB makes direct contact with a short colinear region of T, i.e., residues 102 to 115, previously implicated in both transformation and RB binding.
先前已经证明,猿猴病毒40大T抗原和腺病毒E1A蛋白可与视网膜母细胞瘤易感基因产物(RB)形成复合物。我们研究了这些蛋白在体外与突变型RB蛋白结合的能力。发现RB中跨越第379至792位残基的区域对于与T或E1A结合既必要又充分。此外,RB的该区域包含足够的结构信息,以在区分野生型T和转化缺陷型T突变体K1的能力方面模拟野生型RB。用T中RB结合序列的肽类似物进行的竞争实验结果表明,RB的该区域与T的短共线性区域即先前与转化和RB结合均有关的第102至115位残基直接接触。