DNA binding activities of c-Myc purified from eukaryotic cells.
作者： O Papoulas , N.G. Williams , R.E. Kingston
DOI: 10.1016/S0021-9258(19)50042-4
关键词:
摘要: c-Myc is a nuclear phosphoprotein which contains both leucine zipper and helix-loop-helix dimerization motif. These are adjacent to basic region believed make specific contacts with DNA upon dimerization. We report the purification of full-length near homogeneity from two independent eukaryotic systems: baculovirus overexpression system using an insect cell host, Chinese hamster ovary cells containing heat-inducible c-myc genes. The binding capabilities these preparations were characterized. Both contain distinct activities that bind specifically sequences core CACGTG. Myc protein solely responsible for one activities. Specific bound selected large pool random sequence. Sequencing individual sites by this procedure yielded 12-base consensus, PuACCACGTGCTC, binding. additionally demonstrated complex, copurifying 26-29-kDa protein, higher affinity than alone. Selection complex revealed consensus site similar described above. data demonstrate isolated capable sequence-specific further refine optimal sequence should prove useful in characterizing biochemical properties c-Myc.
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