Nagaoka M, Kuwahara J, Sugiura Y
Institute for Chemical Research, Kyoto University, Japan.
Biochem Biophys Res Commun. 1993 Aug 16;194(3):1515-20. doi: 10.1006/bbrc.1993.1996.
Transcription factor Sp1, which has a DNA binding domain composed of three zinc fingers, binds to GC box (consensus sequence, G/T-GGGCGG-G/A-G/A-C/T) and activates the transcription by RNA polymerase II. Metal substitution of nickel(II) for zinc(II) in Sp1 causes no differences in the mode of protein-DNA interaction. However, sequence preference of Ni(II)Sp1 changes from 5'-GGGGCGGGGC to 5'-GGGGCGTGGC, and is distinct from that of Zn(II)Sp1. The result indicates an important effect of metal-induced folding on sequence-specific recognition of DNA by zinc-finger proteins.
转录因子Sp1具有由三个锌指组成的DNA结合结构域，它与GC盒（共有序列，G/T-GGGCGG-G/A-G/A-C/T）结合并激活RNA聚合酶II的转录。Sp1中用镍（II）取代锌（II）进行金属置换不会导致蛋白质-DNA相互作用模式的差异。然而，Ni（II）Sp1的序列偏好从5'-GGGGCGGGGC变为5'-GGGGCGTGGC，并且与Zn（II）Sp1的不同。结果表明金属诱导的折叠对锌指蛋白对DNA的序列特异性识别具有重要影响。
