METAL-DEPENDENT FOLDING OF A SINGLE ZINC FINGER FROM TRANSCRIPTION FACTOR-IIIA
METAL-DEPENDENT FOLDING OF A SINGLE ZINC FINGER FROM TRANSCRIPTION FACTOR-IIIA
复制标题
DOI：
10.1073/pnas.84.14.4841
复制
发表时间：
1987-07-01
影响因子：
11.1
通讯作者：
PABO, CO
中科院分区：
文献类型：
--
作者：
FRANKEL, AD;BERG, JM;PABO, CO
合成并纯化了与转录因子IIIA的第二个“锌指”结构域相对应的30个氨基酸的多肽。该肽在锌存在下折叠：加入锌显著改变圆二色谱，锌离子保护该肽不被胰酶消化。多肽还与Co2+结合，Co2+络合物的吸收光谱表明，两个半胱氨酸和两个组氨酸形成了一个四面体结合部位。在较高温度(60-75度)下进行实验C)表明这些折叠的金属-多肽络合物具有很好的热稳定性。该多肽在DNA酶和甲基化保护实验中显示出一些序列特异性的作用。然而，它并没有给出一个明确的“足迹”，而且在没有添加锌的情况下观察到了一些影响。
A 30-amino acid peptide, which corresponds to the second "zinc finger" domain of transcription factor IIIA, has been synthesized and purified. This peptide folds in the presence of zinc: adding Zn2+ significantly changes the circular dichroism spectrum, and Zn2+ protects the peptide from tryptic digestion. The peptide also binds Co2+, and the absorption spectrum of the Co2+ complex suggests that a tetrahedral binding site is formed by two cysteines and two histidines. Experiments at higher temperatures (60-75.degree. C) suggest that these folded metal-peptide complexes are quite thermostable. The peptide shows some sequence-specific effects in DNase and methylation protection experiments. However, it does not give a clear "footprint," and some effects are observed in the absence of added zinc.