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Tau protein binds single‐stranded DNA sequence specifically – the proof obtained in vitro with non‐equilibrium capillary electrophoresis of equilibrium mixtures
Author(s) -
Krylova Svetlana M.,
Musheev Michael,
Nutiu Razvan,
Li Yingfu,
Lee Gloria,
Krylov Sergey N.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.01.032
Subject(s) - capillary electrophoresis , dna , chemistry , electrophoresis , dissociation (chemistry) , dissociation constant , equilibrium constant , biophysics , in vitro , gel electrophoresis , biochemistry , chromatography , biology , receptor
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.