Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872709 | FEBS Letters | 2005 | 5 Pages |
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.
Keywords
IPTGEGTAPMSFKinetic capillary electrophoresisEMSAssDNA-binding proteinSSBKCENECEEMpiperazine-N,N′-bis(2-ethanesulfonic acid)Electrophoretic mobility shift assayethylene glycol-bis(β-aminoethyl ether)-N,N,N′,N′-tetraacetic acidinternal standardAlzheimer diseaseProtein–DNA interactionphenylmethylsulfonyl fluoridePipesSingle-stranded DNA binding proteinTau protein
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Svetlana M. Krylova, Michael Musheev, Razvan Nutiu, Yingfu Li, Gloria Lee, Sergey N. Krylov,