Saegusa N, Yokono M, Matsushita K, Sugiura Y
Institute for Chemical Research, Kyoto University, Japan.
Nucleic Acids Symp Ser. 1997(37):151-2.
To clarify binding properties of the first zinc finger of Sp1, finger 1, to GC-box DNA, two-finger mutant peptides Sp1 (zf12) and Sp1 (zf23) were created and their DNA binding characteristics have been compared with those of native three-zinc finger protein Sp1. Some gel electrophoretic experiments involving DNase I footprinting and gel mobility shift assays reveal that finger 1 is not essential to sequence-specific DNA recognition, but moderately contributes to total binding affinity and overall sequence specificity by three zinc fingers of Sp1.
为阐明Sp1的首个锌指（即锌指1）与GC盒DNA的结合特性，构建了双指突变肽Sp1（zf12）和Sp1（zf23），并将它们的DNA结合特性与天然三锌指蛋白Sp1的特性进行了比较。一些涉及DNase I足迹法和凝胶迁移率变动分析的凝胶电泳实验表明，锌指1对序列特异性DNA识别并非必不可少，但对Sp1的三个锌指的总结合亲和力和整体序列特异性有一定贡献。
