Chittenden T, Livingston D M, Kaelin W G
Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
Cell. 1991 Jun 14;65(6):1073-82. doi: 10.1016/0092-8674(91)90559-h.
A DNA-binding site selection and enrichment procedure revealed a sequence-specific DNA-binding activity selectively associated with glutathione S-transferase-retinoblastoma protein chimeras (GST-RB) that had been incubated with a human cell extract. Appropriate mutant forms of GST-RB, incubated in equivalent extracts, did not associate with this specific DNA-binding activity, and a peptide replica of the HPV E7 RB-binding segment selectively inhibited the association of GST-RB with the sequence-specific DNA-binding protein(s). Sequence analysis of oligonucleotides with high affinity for GST-RB complexes, as well as the results of competition binding studies, strongly suggest that RB can associate specifically with the transcription factor E2F or with a protein having closely related DNA-binding properties.
一种DNA结合位点选择与富集程序揭示了一种序列特异性DNA结合活性，该活性与已与人细胞提取物孵育的谷胱甘肽S-转移酶-视网膜母细胞瘤蛋白嵌合体（GST-RB）选择性相关。在等量提取物中孵育的适当突变形式的GST-RB不与这种特异性DNA结合活性相关，并且人乳头瘤病毒E7 RB结合片段的肽复制品选择性抑制GST-RB与序列特异性DNA结合蛋白的结合。对与GST-RB复合物具有高亲和力的寡核苷酸的序列分析以及竞争结合研究的结果强烈表明，RB可以与转录因子E2F或与具有密切相关DNA结合特性的蛋白质特异性结合。
