Alex R, Sözeri O, Meyer S, Dildrop R
Institute for Genetics, University of Cologne, Germany.
Nucleic Acids Res. 1992 May 11;20(9):2257-63. doi: 10.1093/nar/20.9.2257.
The DNA-binding domain of the murine N-Myc protein, comprising the basic helix-loop-helix-zipper (bHLH-zip) region was expressed as a fusion protein in E. coli. The affinity purified glutathione-S-transferase-N-Myc fusion protein (GST-N-MYC) was used to select the N-Myc specific DNA-recognition motif from a pool of random-sequence oligonucleotides. After seven rounds of binding-site selection, specifically enriched oligonucleotides were cloned and sequenced. Of 31 individual oligonucleotides whose sequences were determined, 30 contained a common DNA-motif, defining the hexameric consensus sequence CACGTG. We confirm by mutational analysis that binding of the N-Myc derived bHLH-zip domain to this motif is sequence-specific.
鼠源N-Myc蛋白的DNA结合结构域,包含碱性螺旋-环-螺旋-拉链(bHLH-zip)区域,在大肠杆菌中作为融合蛋白表达。亲和纯化的谷胱甘肽-S-转移酶-N-Myc融合蛋白(GST-N-MYC)用于从随机序列寡核苷酸库中筛选N-Myc特异性DNA识别基序。经过七轮结合位点筛选后,对特异性富集的寡核苷酸进行克隆和测序。在测定序列的31个单独寡核苷酸中,30个含有共同的DNA基序,确定了六聚体共有序列CACGTG。我们通过突变分析证实,源自N-Myc的bHLH-zip结构域与该基序的结合具有序列特异性。