Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 60, Issue 2, Pages 413-421Publisher
SPRINGER BASEL AG
DOI: 10.1007/s000180300034
Keywords
human neuronal tau; nuclear tau; DNA; DNA-binding protein; double-stranded DNA; electrophoretic; mobility shift assay
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Funding
- NIA NIH HHS [AG05892, AG08076] Funding Source: Medline
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Tau, a major microtubule-associated protein of the neuron, which is known to promote the assembly of and to stabilize microtubules, has also been seen associated with chromatin in neuronal cell lines, but its role in this subcellular compartment is still unknown. In this study, the binding of tau to DNA was investigated using the electrophoretic mobility shift assay. Using polynucleotide as probe, we found that tau bound to double-stranded but not to single-stranded DNA. Formation of tau-polynucleotide complex was disrupted by alkaline pH and a high concentration of NaCl, but was not affected by dithiothreitol. Electron microscopy revealed that the protein associated with the nucleic acid in a necklacelike manner. DNA-cellulose chromatography and radioimmunodot-blot analyses showed that calf thymus histones VI-S, VII-S and VIII-S could replace both recombinant human brain tau(352) (tau-23) and tau(441) (tau-40) from DNA. Thus, tau appears to bind to DNA reversibly in the presence of histones.
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