Tau protein binds single‐stranded DNA sequence specifically – the proof obtained in vitro with non‐equilibrium capillary electrophoresis of equilibrium mixtures
Open accessAbstract
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.
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Tau has the capacity to bind DNA and may protect it from oxidative damage.
“Tau has the capacity to bind DNA (281,304) and may protect it from oxidative damage (305).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [304]
In vitro and in cultured cells, tau binds the minor groove of the DNA double helix.
“In vitro and in cultured cells, tau binds the minor groove of the DNA double helix”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [46]
Tau is thought to protect DNA from oxidative damage.
“and is thought to protect DNA from oxidative damage46-48”
From Tau promotes neurodegeneration through global chromatin relaxation (2014) · cites this paper as [46]
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- Authors
- Krylova, S. M., Musheev, M., Nutiu, R., Li, Y., Lee, G., & Krylov, S. N.
- Affiliations
- York University (CA)
- McMaster University (CA)
- University of Iowa (US)
- Corresponding author
- Krylov, Sergey N.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2005-01-28
- Volume
- 579
- Issue
- 6
- Pages
- 1371-1375
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2058989808
- Cited by
- 96
- References
- 0
- Citations by year
- 2025: 4 · 2024: 4 · 2023: 6 · 2022: 3 · 2021: 8 · 2020: 5 · 2019: 8 · 2018: 6 · 2017: 6 · 2016: 3 · 2015: 7 · 2014: 6 · 2013: 1 · 2012: 3
- FWCI
- 4.01
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- FEBS Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Physical Sciences › Engineering › Biomedical Engineering › Microfluidic and Capillary Electrophoresis Applications
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- tau protein, single-stranded DNA, double-stranded DNA, protein-DNA interactions, sequence-specific binding, equilibrium dissociation constant, microtubule-associated proteins
- MeSH terms
- Animals, Base Sequence, DNA, Single-Stranded, Escherichia coli, Protein Binding, Substrate Specificity, Thermodynamics, tau Proteins, Electrophoresis, Capillary
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