1. A nuclear factor that binds purine-rich, single-stranded oligonucleotides derived from S1-sensitive elements upstream of the CFTR gene and the MUC1 gene.
- Author
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Hollingsworth MA, Closken C, Harris A, McDonald CD, Pahwa GS, and Maher LJ 3rd
- Subjects
- Base Sequence, Binding, Competitive, Cystic Fibrosis Transmembrane Conductance Regulator, DNA, Single-Stranded chemistry, DNA, Single-Stranded metabolism, Humans, Hydrogen-Ion Concentration, Molecular Sequence Data, Mucin-1, Nucleic Acid Conformation, Oligodeoxyribonucleotides chemistry, Purines metabolism, Repetitive Sequences, Nucleic Acid, Single-Strand Specific DNA and RNA Endonucleases metabolism, Trans-Activators metabolism, Tumor Cells, Cultured, Ultraviolet Rays, Cystic Fibrosis genetics, Membrane Glycoproteins genetics, Mucins genetics, Nuclear Proteins metabolism, Oligodeoxyribonucleotides metabolism
- Abstract
We have identified two regions of non-random purine/pyrimidine strand asymmetry that were nearly identical in sequence in the 5' flanking (promoter) regions of the human cystic fibrosis transmembrane conductance regulator (CFTR) gene and the human MUC1 gene. These regions contain perfect mirror repeat elements, a sequence motif previously found to be associated with the formation of H-DNA conformations. In this report we demonstrate that a single-stranded non-B DNA conformation exists at low pH in supercoiled plasmids containing the similar mirror repeat elements, and that S1 nuclease digestion maps the single-stranded region to the position of the mirror repeats. In addition, we identify a nuclear protein of approximately 27 kD that binds to single-stranded oligonucleotides corresponding to the purine-rich strand of this region, but not to the pyrimidine-rich strands or to double-stranded oligonucleotides with corresponding purine/pyrimidine strand asymmetry.
- Published
- 1994
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