DNA bending is an important component of site-specific recognition by the TATA binding protein.
DNA bending is an important component of site-specific recognition by the TATA binding protein.
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DOI：
10.1006/jmbi.1995.0388
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发表时间：
1995-07
影响因子：
5.6
通讯作者：
Barry D. Starr;Barbara C. Hoopes;Diane K. Hawley
中科院分区：
文献类型：
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作者：
Barry D. Starr;Barbara C. Hoopes;Diane K. Hawley
我们已经使用凝胶电泳方法来分析由TATA结合蛋白（TBP）结合到共有TATA盒序列后诱导的DNA弯曲的程度、位置和方向。我们的观察结果与TBP-TATA盒复合物的X射线晶体结构的模型一致。我们还测量了TBP在结合许多变体TATA盒序列时诱导的弯曲的大小和方向，我们已经测量了TBP结合亲和力。我们发现，DNA在复合物中弯曲的程度在不同的序列之间存在差异，并且与复合物的稳定性相关;也就是说，复合物的稳定性越高，TBP弯曲的DNA就越多。这项研究提供了第一个证据，TBP-DNA复合物的结构可能会因不同的DNA序列而异。此外，我们建议，根据我们的研究结果，弯曲的能量显著有助于TBP对不同序列的整体结合亲和力。
We have used gel electrophoretic methods to analyze the extent, location and direction of the DNA bend induced by the TATA binding protein (TBP) upon binding to a consensus TATA box sequence. Our observations were consistent with the proposed models for the X-ray crystal structure of the TBP-TATA box complex. We have also measured the magnitude and direction of the bend induced by TBP upon binding a number of variant TATA box sequences for which we have measured TBP binding affinity. We found that the extent to which the DNA was bent in the complex differed among the various sequences and was correlated with the stability of the complex; that is, the greater the stability of the complex, the more the DNA appeared to be bent by TBP. This study provides the first evidence that the structure of the TBP-DNA complex may vary with different DNA sequences. In addition, we propose, based on our findings, that the energetics of bending contribute significantly to the overall binding affinity of TBP for different sequences.