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首页> 外文期刊>Biochemistry >Protein-DNA binding correlates with structural thermostability for thefull-length human p53 protein
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Protein-DNA binding correlates with structural thermostability for thefull-length human p53 protein

机译：蛋白-DNA结合与全长人p53蛋白的结构热稳定性相关

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摘要

Full-length p53 protein purified from Escherichia coli in the unmodified, "latent" form was examined by several methods to correlate thermal stability of structure with functional DNA binding. Structure prediction algorithms indicate that the majority of beta -sheet structure occurs in the p53 core DNA binding domain. Circular dichroism spectra demonstrate that the intact protein is surprisingly stable with a midpoint for the irreversible unfolding transition at similar to 73 degreesC. Significant beta -sheet structural signal remains even to 100 degreesC. The persistent beta -sheet CD signal correlates with significant DNA binding (K-d similar to nM range) to temperatures as high as 50 degreesC. These data confirm the ability of the DNA binding domain in the full-length "latent" protein to bind consensus dsDNA targets effectively in the absence of activators over a broad temperature range. In addition, we demonstrate that Ab1620 reactivity is not directly correlated with the functional activity of the full-length protein since loss of this epitope occurs at temperatures at which significant specific DNA binding can still be measured.
机译：通过几种方法检查了从大肠杆菌中纯化的未修饰的“潜伏”形式的全长p53蛋白，以将结构的热稳定性与功能性DNA结合相关联。结构预测算法表明，大多数β-sheet结构出现在p53核心DNA结合域中。圆二色性光谱表明，完整的蛋白质出乎意料地稳定，在类似于73摄氏度时具有不可逆的展开过渡的中点。明显的β-折叠结构信号甚至保持到100℃。持续的β-sheetCD信号与显着的DNA结合（K-d类似于nM范围）与高达50摄氏度的温度相关。这些数据证实了全长“潜伏”蛋白中DNA结合结构域在宽广温度范围内不存在活化剂的情况下有效结合共有dsDNA靶标的能力。此外，我们证明Ab1620反应性与全长蛋白的功能活性不直接相关，因为此表位的丢失发生在仍然可以检测到明显的特异性DNA结合的温度下。

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