Xu J, Koudelka G B
Department of Biological Sciences, State University of New York, Buffalo, New York 14260-1300, USA.
J Biol Chem. 1998 Sep 11;273(37):24165-72. doi: 10.1074/jbc.273.37.24165.
As detected by chemical nuclease treatments, the conformation of the 434 repressor-DNA complex depends on the sequence of the bound DNA (Bell, A. C., and Koudelka, G. B. (1993) J. Mol. Biol. 234, 542-553). We show here that these DNA sequence-dependent conformational changes alter the efficiency with which the repressor activates transcription from 434 PRM. Several lines of evidence suggest that binding site sequence affects the repressor's ability to activate transcription by altering the accessibility of the activation surface on the repressor to RNA polymerase. The results presented here show that in addition to affecting transcription by altering the overall binding affinity of protein for DNA, DNA sequence may also modulate the activity of the DNA-bound protein.
通过化学核酸酶处理检测发现，434阻遏蛋白-DNA复合物的构象取决于所结合DNA的序列（贝尔，A.C.，和库德尔卡，G.B.（1993年）《分子生物学杂志》234卷，542 - 553页）。我们在此表明，这些依赖于DNA序列的构象变化改变了阻遏蛋白激活434 PRM转录的效率。几条证据线索表明，结合位点序列通过改变阻遏蛋白上激活表面对RNA聚合酶的可及性来影响其激活转录的能力。此处给出的结果表明，除了通过改变蛋白质与DNA的总体结合亲和力来影响转录外，DNA序列还可能调节与DNA结合的蛋白质的活性。
