Kinetic analysis of the Ku-DNA binding activity reveals a redox-dependent alteration in protein structure that stimulates dissociation of the Ku-DNA complex
Open accessAbstract
Ku is a heterodimeric protein comprising 70- and 80-kDa subunits that participate in the non-homologous end-joining (NHEJ) repair pathway for rejoining DNA double strand breaks. We have analyzed the pre-steady state binding of Ku with various DNA duplex substrates and identified a redox-sensitive Ku-DNA interaction. Pre-steady state analysis of Ku DNA binding was monitored via intrinsic Ku quenching upon binding DNA and revealed that, under fully reduced conditions, binding occurred in a single-step process. Reactions performed under limited reduction revealed a two-step binding process, whereas under fully oxidized conditions, we were unable to detect quenching of Ku fluorescence upon binding DNA. The differential quenching observed under the different redox conditions could not be attributed to two Ku molecules binding to a single substrate or Ku sliding inward on the substrate. Although only modest differences in Ku DNA binding activity were observed in the stoichiometric anisotropy and electrophoretic mobility shift assay studies, as a function of redox conditions, a dramatic difference in the rate of Ku dissociation from DNA was observed. This effect was also induced by diamide treatment of Ku and could be abrogated by dithiothreitol treatment, demonstrating a reversible redox effect on the stability of the Ku-DNA complex. The redox-dependent alteration in Ku-DNA interactions is manifested by a redox-dependent alteration in Ku structure, which was confirmed by limited proteolysis and mass spectrometry analyses. The results support a model for the interaction of Ku with DNA that is regulated by redox status and is achieved by altering the dissociation of the Ku-DNA complex.
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The Ku70/Ku80 heterodimer is the first protein to bind to the end of a double-strand break.
“The very first protein to bind to the end of the double-strand break is the Ku70/Ku80 heterodimer.”
From Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis (2012) · cites this paper as [57]
Ku70/Ku80 forms a preformed channel that slides onto DNA termini, causing a conformational change in Ku under both redox and DNA binding conditions.
“This unique protein forms a preformed channel so that it slides onto the DNA termini, causing a conformational change in Ku under both redox and DNA binding conditions [57,58].”
From Integration of DNA damage and repair with murine double-minute 2 (Mdm2) in tumorigenesis (2012) · cites this paper as [57]
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A systems biology approach to DNA damage repair
Dolan, D. (2013)
- Authors
- Andrews, B. J., Lehman, J. A., & Turchi, J. J.
- Affiliations
- Indiana University School of Medicine (US)
- Wright State University (US)
- Indiana University Indianapolis (US)
- Corresponding author
- Turchi, John J.
- ORCID
- Turchi, John J.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2006-05
- Volume
- 281
- Issue
- 19
- Pages
- 13596-13603
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2432111
- OpenAlex
- W2051663745
- Cited by
- 49
- References
- 38
- Citations by year
- 2025: 2 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 4 · 2017: 2 · 2016: 1 · 2015: 4 · 2013: 3 · 2012: 9
- FWCI
- 0.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- IUScholarWorks (Indiana University) (submittedVersion)
- Funders
- U.S. Department of Defense
- National Institutes of Health
- National Cancer Institute (CA82741, R01CA082741)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
- Keywords
- Ku protein, redox regulation, non-homologous end joining, DNA double-strand break repair, pre-steady-state kinetics, fluorescence quenching, protein structure, diamide, dithiothreitol, limited proteolysis, Ku80, Ku70
- MeSH terms
- Ku Autoantigen, DNA, DNA Helicases, Humans, Kinetics, Oxidation-Reduction, Protein Binding, Protein Conformation
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