Encyclopedia of Cancer

Living Edition
| Editors: Manfred Schwab

γH2AX

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27841-9_2713-2

Synonyms

Definition

H2AX is one of the histone proteins that is systematically found and ubiquitously distributed throughout the genome. DNA double-strand breaks (DSBs) induce rapid phosphorylation of H2AX (142 amino acids) at serine 139, a highly conserved serine residue located in the C-terminus.

Characteristics

In eukaryotes, DNA is highly condensed and packaged into chromatin within the nuclei. This condensed chromatin forms a structural barrier for DNA processing during DNA repair, replication, transcription, and recombination. A fundamental subunit of the chromosome is the nucleosome, which is composed of 146 bp of DNA wrapped in two complete turns around an octamer of the core histones H2A, H2B, H3, and H4, and there are varying lengths of linker DNA connecting these subunits. The core histone octamer forms a 100-kDa protein complex. Histone H2A has been conserved throughout eukaryotic evolution. There are three H2A subfamilies:...

Keywords

Comet Assay Base Excision Repair Replication Fork Ataxia Telangiectasia Nijmegen Breakage Syndrome 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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References

  1. Bassing CH, Alt FW (2004) H2AX may function as an anchor to hold broken chromosomal DNA ends in close proximity. Cell Cycle 3:149–153CrossRefPubMedGoogle Scholar
  2. Fernandez-Capetillo O, Lee A, Nussenzweig M et al (2004) H2AX: the histone guardian of the genome. DNA Repair 3:959–967CrossRefPubMedGoogle Scholar
  3. Stucki M, Jackson SP (2006) γH2AX and MDC1: anchoring the DNA-damage-response machinery to broken chromosomes. DNA Repair 5:534–543CrossRefPubMedGoogle Scholar
  4. Takahashi A, Ohnishi T (2005) Does γH2AX foci formation depend on the presence of DNA double strand breaks? Cancer Lett 229:171–179, Erratum in: 236: 155–156CrossRefPubMedGoogle Scholar

Copyright information

© Springer-Verlag Berlin Heidelberg 2015

Authors and Affiliations

  • Takeo Ohnishi
    • 1
  • Eiichiro Mori
    • 1
  • Akihisa Takahashi
    • 2
  1. 1.Department of Radiation Oncology, School of MedicineNara Medical UniversityKashiharaJapan
  2. 2.Heavy Ion Medical CenterGunma UniversityMaebashiJapan