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

FEBS Lett. 2005 Feb 28;579(6):1371-5. doi: 10.1016/j.febslet.2005.01.032. Epub 2005 Jan 28.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • DNA, Single-Stranded / genetics
  • DNA, Single-Stranded / metabolism*
  • Electrophoresis, Capillary
  • Escherichia coli
  • Protein Binding
  • Substrate Specificity
  • Thermodynamics
  • tau Proteins / metabolism*

Substances

  • DNA, Single-Stranded
  • tau Proteins