4.5 Article

Tau protein binds single-stranded DNA sequence specifically - the proof obtained in vitro with non-equilibrium capillary electrophoresis of equilibrium mixtures

Journal

FEBS LETTERS
Volume 579, Issue 6, Pages 1371-1375

Publisher

WILEY
DOI: 10.1016/j.febslet.2005.01.032

Keywords

tau protein; protein-DNA interaction; Alzheimer disease; non-equilibrium capillary electrophoresis of equilibrium mixture; ssDNA-binding protein

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Tau is a microtubule-associated protein, which plays an important role in physiology and pathology of neurons. Tau has been recently reported to bind double-stranded DNA (dsDNA) but not to bind single-stranded DNA (ssDNA) [Cell. Mol. Life Sci. 2003, 60, 413-421]. Here, we prove that tau binds not only dsDNA but also ssDNA. This finding was facilitated by using two kinetic capillary electrophoresis methods: (i) non-equilibrium capillary electrophoresis of equilibrium mixtures (NECEEM); (ii) affinity-mediated NECEEM. Using the new approach, we observed, for the first time, that tau could induce dissociation of strands in dsDNA by binding one of them in a sequence-specific fashion. Moreover, we determined the equilibrium dissociation constants for all tau-DNA complexes studied. (C) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

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