Desjarlais J R, Berg J M
Thomas C. Jenkins Department of Biophysics, Johns Hopkins University, Baltimore, Maryland 21218.
Proteins. 1992 Feb;12(2):101-4. doi: 10.1002/prot.340120202.
A peptide corresponding to the three zinc finger domains of the human transcription factor Sp1 has been expressed and found to bind a consensus Sp1 binding site with the sequence 5'-GGGGCGGGG-3'. Examination of the amino acid distributions within a large zinc finger sequence data base and chemical arguments suggested that a particular Arg to Gln sequence change might convert binding specificity to 5'-GGGGCAGGG-3'. Experimental tests of this hypothesis revealed that such a change could be induced only when two other sequence changes, deduced from examination of sequence correlations, were made as well. These results provide the most direct information to date about how zinc finger proteins might recognize adenine-containing binding sites and bear on the existence and nature of any code between zinc finger protein and binding site sequences.
一种与人类转录因子Sp1的三个锌指结构域相对应的肽已被表达，并发现它能与序列为5'-GGGGCGGGG-3'的共有Sp1结合位点结合。对一个大型锌指序列数据库中氨基酸分布的研究以及化学分析表明，特定的精氨酸到谷氨酰胺的序列变化可能会将结合特异性转变为5'-GGGGCAGGG-3'。对这一假设的实验测试表明，只有当通过序列相关性分析推导得出的另外两个序列变化也同时发生时，这种变化才可能被诱导。这些结果提供了迄今为止关于锌指蛋白如何识别含腺嘌呤结合位点的最直接信息，并与锌指蛋白和结合位点序列之间任何编码的存在及性质相关。
