Abstract
Phosphorylation of the human histone variant H2A.X and H2Av, its homolog in Drosophila melanogaster, occurs rapidly at sites of DNA double-strand breaks. Little is known about the function of this phosphorylation or its removal during DNA repair. Here, we demonstrate that the Drosophila Tip60 (dTip60) chromatin-remodeling complex acetylates nucleosomal phospho-H2Av and exchanges it with an unmodified H2Av. Both the histone acetyltransferase dTip60 as well as the adenosine triphosphatase Domino/p400 catalyze the exchange of phospho-H2Av. Thus, these data reveal a previously unknown mechanism for selective histone exchange that uses the concerted action of two distinct chromatin-remodeling enzymes within the same multiprotein complex.
MeSH terms
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Acetyl Coenzyme A / metabolism
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Acetylation
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Acetyltransferases / genetics
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Acetyltransferases / metabolism*
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Adenosine Triphosphatases / metabolism
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Animals
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Cell Line
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DNA Damage*
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DNA Repair
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Dimerization
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Drosophila Proteins / genetics
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Drosophila Proteins / metabolism
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Drosophila melanogaster / embryology
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Drosophila melanogaster / genetics
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Drosophila melanogaster / metabolism*
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Embryo, Nonmammalian / metabolism
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Histone Acetyltransferases
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Histones / metabolism*
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Multiprotein Complexes / metabolism*
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Nucleosomes / metabolism*
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Phosphorylation
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RNA Interference
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Recombinant Proteins / metabolism
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Transcription Factors / metabolism
Substances
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Drosophila Proteins
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Histones
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Multiprotein Complexes
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Nucleosomes
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Recombinant Proteins
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Transcription Factors
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Acetyl Coenzyme A
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Acetyltransferases
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Histone Acetyltransferases
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Adenosine Triphosphatases