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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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.
|
| skos:exactMatch | |
| uniprot:name |
Science
|
| uniprot:author |
Abmayr S.M.,
Florens L.,
Glaser R.L.,
Kusch T.,
Macdonald W.H.,
Swanson S.K.,
Washburn M.P.,
Workman J.L.,
Yates J.R. III
|
| uniprot:date |
2004
|
| uniprot:pages |
2084-2087
|
| uniprot:title |
Acetylation by Tip60 is required for selective histone variant exchange at DNA lesions.
|
| uniprot:volume |
306
|
| dc-term:identifier |
doi:10.1126/science.1103455
|