Effect of Phosphorylation and Aggregation on Tau Binding to Dna
Abstract
The potential function of neuronal tau was found by our recent studies on the effect of tau on the melting temperature of both calf thymus DNA and plasmid pBluescript-II SK (Hua and He, Chin. Sci. Bull. 2000, 45:999-1001). Herein we examined whether or not the interaction of tau with DNA was related to phosphorylation and aggregation. Tau, phosphorylated by neuronal cdc2-like kinase, associated with DNA as shown by electrophoretic mobility shift assay. Similar to native tau, phosphorylated tau could increase the melting temperature of calf thymus DNA. When tau was aggregated or treated with formaldehyde, neither native tau nor phosphorylated tau kept its ability to interact with DNA, suggesting that binding of tau to DNA was in an aggregation-dependent, and a phosphorylation-independent, manner.
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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 [281]
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Tau protein binds to pericentromeric DNA: a putative role for nuclear tau in nucleolar organization
Sjöberg, M. K., Shestakova, E., Mansuroglu, Z., Maccioni, R. B., & Bonnefoy, E. (2006) · Journal of Cell Science · doi:10.1242/jcs.02907 · Cited by 166 · see citing works
Nuclear Tau and Its Potential Role in Alzheimer’s Disease
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“Our laboratory generated a model of tauopathy in Drosophila melanogaster by expressing human wild-type full-length (2N/4R) tau in the eye using a direct fusion construct of the human tau cDNA to the eye-specific glass (gl) promoter (gl-tau fly).”
BackgroundInfluential
- Authors
- Hua, Q., & He, R.-Q.
- Affiliations
- Chinese Academy of Sciences (CN)
- ORCID
- Hua, Qian
- Venue
- Protein & Peptide Letters
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2002-08-01
- Volume
- 9
- Issue
- 4
- Pages
- 349-357
- ISSN
- 0929-8665 (ISSN-L)
- OpenAlex
- W2108606653
- Cited by
- 53
- References
- 0
- Citations by year
- 2025: 5 · 2024: 3 · 2023: 2 · 2022: 2 · 2021: 2 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 6 · 2016: 2 · 2015: 4 · 2014: 3 · 2013: 5 · 2012: 1
- FWCI
- 1.00
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Protein and Peptide Letters (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- tau protein, DNA binding, phosphorylation, protein aggregation, Cdc2-like kinases, calf thymus DNA, DNA melting temperature, formaldehyde crosslinking
- MeSH terms
- Animals, Cattle, DNA, DNA-Binding Proteins, Hot Temperature, Humans, Neurons, Phosphorylation, Protein Denaturation, Recombinant Proteins, tau Proteins
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