Peer-Reviewed Journal Details
Mandatory Fields
Brown, JAL,Eykelenboom, JK,Lowndes, NF
2012
December
FEBS open bio
Co-mutation of histone H2AX S139A with Y142A rescues Y142A-induced ionising radiation sensitivity
Published
Optional Fields
H2AX Y142 S139 DSB IR 53BP1
2
313
317
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. (C) 2012 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
10.1016/j.fob.2012.09.008
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