Purification and characterization of a DNA-binding protein activated by ionizing radiation.
作者： B Teale , S Singh , K.K. Khanna , D Findik , M.F. Lavin
DOI: 10.1016/S0021-9258(19)50017-5
关键词:
摘要: Exposure of mammalian cells to a variety agents leads the activation pre-existing proteins and induction specific genes. We have recently described appearance DNA-binding protein in nuclei from exposed ionizing radiation (Singh, S. P., Lavin, M. F. (1990) Mol. Cell. Biol. 10, 5279-5285). This is present cytoplasm unperturbed apparently translocated nucleus response damage. describe here purification characterization this protein. Purification involved use affinity chromatography employing multimeric form motif conjugated cyanogen bromide-activated Sepharose. Three species were recognized by UV-cross-linking South-Western analysis. The major or that with highest was approximately 70 kDa size. DNase-1 footprint analysis revealed single binding site kappa immunoglobulin gene enhancer putative control sequence upstream c-myc gene. At salt concentrations as high 1 M, up 40% activity maintained Kd calculated be 1.205 x 10(-6) M-1. Binding found modulated phosphorylation. Removal phosphate groups resulted loss activity. It not clear at stage whether factor(s) plays role transcription more general DNA-processing
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