In this study, the binding oftau to DNA is investi-gated by the electrophoretic mobility shift assay. Using polynucleotide as probe, we find that tau bound to dou-ble-stranded DNA but not to single-stranded DNA. For-m...In this study, the binding oftau to DNA is investi-gated by the electrophoretic mobility shift assay. Using polynucleotide as probe, we find that tau bound to dou-ble-stranded DNA but not to single-stranded DNA. For-mation of tau-polynucleotide complex is interfered at alkaline pH and high concentration of NaCl, but is not affected by dithiothreiotol. Electron microscopy reveals that the protein associated with the nucleic acid in a necklace manner. Nevertheless,展开更多
文摘In this study, the binding oftau to DNA is investi-gated by the electrophoretic mobility shift assay. Using polynucleotide as probe, we find that tau bound to dou-ble-stranded DNA but not to single-stranded DNA. For-mation of tau-polynucleotide complex is interfered at alkaline pH and high concentration of NaCl, but is not affected by dithiothreiotol. Electron microscopy reveals that the protein associated with the nucleic acid in a necklace manner. Nevertheless,
