Co-mutation of histone H2AX S139A with Y142A rescues Y142A-induced ionising radiation sensitivity

James A.L. Brown, John K. Eykelenboom, Noel F. Lowndes

Research output: Contribution to journalArticlepeer-review

Abstract

Under normal conditions histone H2AX is constitutively phosphorylated on tyrosine (Y) 142 by Williams-Beuren syndrome transcription factor kinase (WSTF). Following DNA double strand breaks (DSB), Y142 is de-phosphorylated and serine (S) 139 is phosphorylated. Here we explored DSB-dependent cross talk between H2AX residues S139 and Y142. H2axY142A mutation resulted in increased sensitivity to ionising radiation (IR), compared to H2axS139A. Interestingly, co-mutation of S139A and Y142A rescued IR sensitivity. The DSB response proteins 53Bp1 and Rad51 were recruited to IR-induced foci (IRIF) in H2axS139A, H2axY142A and H2axS139A/. Y142A cells. Our results suggest that H2axY142A IR sensitivity is dependent upon the C-terminal residue, S139.

Original languageEnglish
Pages (from-to)313-317
Number of pages5
JournalFEBS Open Bio
Volume2
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • 53BP1
  • DSB
  • H2AX
  • IR
  • S139
  • Y142

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