ArticleNucleic acids research2006
Terminal DNA structure and ATP influence binding parameters of the DNA-dependent protein kinase at an early step prior to DNA synapsis.
Article in Nucleic acids research, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- ERCC6L2 ensures repair fidelity for staggered-end DNA double-strand breaks.Nature communications · 2026Article
- Cryo-EM of NHEJ supercomplexes provides insights into DNA repair.Molecular cell · 2021Article
- The active DNA-PK holoenzyme occupies a tensed state in a staggered synaptic complex.Structure (London, England : 1993) · 2021Article
- Deciphering the role of distinct DNA-PK phosphorylations at collapsed replication forks.DNA repair · 2020Article
- Activation of DNA-PK by hairpinned DNA ends reveals a stepwise mechanism of kinase activation.Nucleic acids research · 2020Article
- Phosphorylation at S2053 in Murine (S2056 in Human) DNA-PKcs Is Dispensable for Lymphocyte Development and Class Switch Recombination.Journal of immunology (Baltimore, Md. : 1950) · 2019Article
- Structure-Specific nuclease activities of Artemis and the Artemis: DNA-PKcs complex.Nucleic acids research · 2016Article
- Resolution of complex ends by Nonhomologous end joining - better to be lucky than good?Genome integrity · 2012Article
- N-terminal constraint activates the catalytic subunit of the DNA-dependent protein kinase in the absence of DNA or Ku.Nucleic acids research · 2012Article
- Coordination of DNA-PK activation and nuclease processing of DNA termini in NHEJ.Antioxidants & redox signaling · 2011Review
- Choosing the right path: does DNA-PK help make the decision?Mutation research · 2011Review
- Phosphorylation: the molecular switch of double-strand break repair.International journal of proteomics · 2011Article
- TRF2/RAP1 and DNA-PK mediate a double protection against joining at telomeric ends.The EMBO journal · 2010Article
- Ku and DNA-dependent protein kinase dynamic conformations and assembly regulate DNA binding and the initial non-homologous end joining complex.The Journal of biological chemistry · 2010Article
- The mechanism of double-strand DNA break repair by the nonhomologous DNA end-joining pathway.Annual review of biochemistry · 2010Review
- A mechanism for DNA-PK activation requiring unique contributions from each strand of a DNA terminus and implications for microhomology-mediated nonhomologous DNA end joining.Nucleic acids research · 2008Article
- Cryo-EM structure of the DNA-dependent protein kinase catalytic subunit at subnanometer resolution reveals alpha helices and insight into DNA binding.Structure (London, England : 1993) · 2008Article
- DNA-PK autophosphorylation facilitates Artemis endonuclease activity.The EMBO journal · 2006Article
- Binding kinetics and activity of human poly(ADP-ribose) polymerase-1 on oligo-deoxyribonucleotide substrates.Journal of molecular recognition : JMRArticle
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The DNA-dependent protein kinase catalytic subunit (DNA-PKcs) regulates the non-homologous end-joining pathway of DNA double-strand break repair in mammalian cells. The ability of DNA-PKcs to sense and respond to different terminal DNA structures is postulated to be important for its regulatory function. It is unclear whether discrimination occurs at the time of formation of the initial protein-DNA complex or later, at the time of formation of a paired, or synaptic complex between opposing DNA ends. To gain further insight into the mechanism of regulation, we characterized the binding of DNA-PKcs to immobilized DNA fragments that cannot undergo synapsis. Results showed that DNA-PKcs strongly discriminates between different terminal structures at the time of initial complex formation. Although Ku protein stabilizes DNA-PKcs binding overall, it is not required for discrimination between terminal structures. Base mispairing, temperature and the presence of an interstrand linkage influence the stability of the initial complex in a manner that suggests a requirement for DNA unwinding, reminiscent of the 'open complex' model of RNA polymerase-promoter DNA interaction. ATP and a nonhydrolyzable ATP analog also influence the stability of the DNA-PKcs*DNA complex, apparently by an allosteric mechanism that does not require DNA-PKcs autophosphorylation.
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