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Nucleic Acids Research, 2002, Vol. 30, No. 17 3698-3705
© 2002 Oxford University Press

DNA double-strand break-induced phosphorylation of Drosophila histone variant H2Av helps prevent radiation-induced apoptosis

James P. Madigan1, Heather L. Chotkowski1 and Robert L. Glaser*,1,2

1 Wadsworth Center, New York State Department of Health and 2 Department of Biomedical Sciences, State University of New York, Albany, NY 12201-2002, USA

*To whom correspondence should be addressed at: Wadsworth Center, New York State Department of Health, PO Box 22002, Albany, NY 12201-2002, USA. Tel: +1 518 473 4201; Fax: +1 518 474 3181; Email: glaser{at}wadsworth.org

The response of eukaryotic cells to the formation of a double-strand break (DSB) in chromosomal DNA is highly conserved. One of the earliest responses to DSB formation is phosphorylation of the C-terminal tail of H2A histones located in nucleosomes near the break. Histone variant H2AX and core histone H2A are phosphorylated in mammals and budding yeast, respectively. We demonstrate the DSB-induced phosphorylation of histone variant H2Av in Drosophila melanogaster. H2Av is a member of the H2AZ family of histone variants. Ser137 within an SQ motif located near the C- terminus of H2Av was phosphorylated in response to {gamma}-irradiation in both tissue culture cells and larvae. Phosphorylation was detected within 1 min of irradiation and detectable after only 0.3 Gy of radiation exposure. Photochemically induced DSBs, but not general oxidative damage or UV-induced nicking of DNA, caused H2Av phosphorylation, suggesting that phosphorylation is DSB specific. Imaginal disc cells from Drosophila expressing a mutant allele of H2Av with its C-terminal tail deleted, and therefore unable to be phosphorylated, were more sensitive to radiation-induced apoptosis than were wildtype controls, suggesting that phosphorylation of H2Av is important for repair of radiation-induced DSBs. These observations suggest that in addition to providing the function of an H2AZ histone, H2Av is also the functional homolog in Drosophila of H2AX.


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