ArticleThe Journal of biological chemistry2010
Phosphorylation of histone H2A.X by DNA-dependent protein kinase is not affected by core histone acetylation, but it alters nucleosome stability and histone H1 binding.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- Equine histones are mobilized within equid alphaherpesvirus 1 (EHV1) replication compartments.Journal of virology · 2025Article
- Structural insights into γH2Ax containing nucleosomes.Nucleic acids research · 2025Article
- Identification of novel H2A histone variants across diverse clades of algae.Genome biology · 2025Article
- Involvement of H2A variants in DNA damage response of zygotes.Cell death discovery · 2024Article
- Histone H2A variant H2A.B is enriched in transcriptionally active and replicating HSV-1 lytic chromatin.Journal of virology · 2024Article
- Mind the gap: Epigenetic regulation of chromatin accessibility in plants.Plant physiology · 2024Review
- Maintaining Genome Integrity: Protein Kinases and Phosphatases Orchestrate the Balancing Act of DNA Double-Strand Breaks Repair in Cancer.International journal of molecular sciences · 2023Review
- Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023Review
- Histone variants H3.3 and H2A.Z/H3.3 facilitate excision of uracil from nucleosome core particles.DNA repair · 2022Article
- Zygotic gene activation in mice: profile and regulation.The Journal of reproduction and development · 2022Review
- PARP1 exhibits enhanced association and catalytic efficiency with γH2A.X-nucleosome.Nature communications · 2019Article
- Distinct roles foreLife · 2019Article
- Ultrastructure of spermiogenesis and the distribution of spermatozoal nuclear histones in the Japanese mantis shrimp, Oratosquilla oratoria (Crustacea: Stomatopoda).Journal of morphology · 2019Article
- Alterations in histone acetylation following exposure toRadiation and environmental biophysics · 2018Article
- Review
- H2A O-GlcNAcylation at serine 40 functions genomic protection in association with acetylated H2AZ or γH2AX.Epigenetics & chromatin · 2017Article
- Nucleosome stability measured in situ by automated quantitative imaging.Scientific reports · 2017Article
- Oxidative Stress Delays Prometaphase/Metaphase of the First Cleavage in Mouse Zygotes via the MAD2L1-Mediated Spindle Assembly Checkpoint.Oxidative medicine and cellular longevity · 2017Article
- DNA damage responsive miR-33b-3p promoted lung cancer cells survival and cisplatin resistance by targeting p21Cell cycle (Georgetown, Tex.) · 2016Article
- mda-7/IL-24 Induces Cell Death in Neuroblastoma through a Novel Mechanism Involving AIF and ATM.Cancer research · 2016Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Phosphorylation of the C-terminal end of histone H2A.X is the most characterized histone post-translational modification in DNA double-stranded breaks (DSB). DNA-dependent protein kinase (DNA-PK) is one of the three phosphatidylinositol 3 kinase-like family of kinase members that is known to phosphorylate histone H2A.X during DNA DSB repair. There is a growing body of evidence supporting a role for histone acetylation in DNA DSB repair, but the mechanism or the causative relation remains largely unknown. Using bacterially expressed recombinant mutants and stably and transiently transfected cell lines, we find that DNA-PK can phosphorylate Thr-136 in addition to Ser-139 both in vitro and in vivo. Furthermore, the phosphorylation reaction is not inhibited by the presence of H1, which in itself is a substrate of the reaction. We also show that, in contrast to previous reports, the ability of the enzyme to phosphorylate these residues is not affected by the extent of acetylation of the core histones. In vitro assembled nucleosomes and HeLa S3 native oligonucleosomes consisting of non-acetylated and acetylated histones are equally phosphorylated by DNA-PK. We demonstrate that the apparent differences in the extent of phosphorylation previously observed can be accounted for by the differential chromatin solubility under the MgCl(2) concentrations required for the phosphorylation reaction in vitro. Finally, we show that although H2A.X does not affect nucleosome conformation, it has a de-stabilizing effect that is enhanced by the DNA-PK-mediated phosphorylation and results in an impaired histone H1 binding.
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