Structure and Function of Histone H2AX

  • David Miguel Susano Pinto
  • Andrew Flaus
Part of the Subcellular Biochemistry book series (SCBI, volume 50)


Histone H2AX is a histone variant found in almost all eukaryotes. It makes a central contribution to genome stability through its role in the signaling of DNA damage events and by acting as a foundation for the assembly of repair foci. The H2AX protein sequence is highly similar and in some cases overlapping with replication-dependent canonical H2A, yet the H2AX gene and protein structures exhibit a number of features specific to the role of this histone in DNA repair. The most well known of these is a specific serine at the extreme C-terminus of H2AX which is phosphorylated by Phosphoinositide-3-Kinase-related protein Kinases (PIKKs) to generate the γH2AX mark. However, recent studies have demonstrated that phosphorylation, ubiquitylation and other post-translational modifications are also crucial for function. H2AX transcript properties suggest a capability to respond to damage events. Furthermore, the biochemical properties of H2AX protein within the nucleosome structure and its distribution within chromatin also point to features linked to its role in the DNA damage response. In particular, the theoretical inter-nucleosomal spacing of H2AX and the potential implications of amino acid residues distinguishing H2AX from canonical H2A in structure and dynamics are considered in detail. This review summarises current understanding of H2AX from a structure–function perspective.


Histone H2AX Structure–function Chromatin structure DSB DNA repair 



double strand break


DNA damage response


histone downstream element


homologous recombination


ionising radiation


non-homologous end joining


phosphoinositide-3-kinase-related protein kinase


post-translation modification


superhelical location


stem–loop binding protein


small nuclear RNA


transcription start site



We thank Prof. Cathal Seoighe for assistance with calculations of random H2AX distribution, Prof. Noel Lowndes for his input and Dr. Kevin Roche for helpful discussions. We gratefully acknowledge the support of Science Foundation Ireland and Health Research Board of Ireland for supporting work in our laboratory. DMSP acknowledges the support of the Portuguese Foundation for Science and Technology (FCT).


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© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Centre for Chromosome BiologySchool of Natural Sciences, National University of IrelandGalwayIreland

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