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http://purl.uniprot.org/citations/15613478http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15613478http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15613478http://www.w3.org/2000/01/rdf-schema#comment"Formation of gamma-H2AX foci is a P. O.cellular response to genotoxic stress, such as DNA double strand breaks or stalled replication forks. Here we show that gamma-H2AX foci were also formed when cells were incubated with 0.5 microg/ml DNA intercalating agent actinomycin D. In untreated cells, gamma-H2AX co-immunoprecipitated with Ku70, a subunit of DNA-dependent protein kinase, as well as with nuclear DNA helicase II (NDH II), a DEXH family helicase also known as RNA helicase A or DHX9. This association was increased manifold after actinomycin D treatment. DNA degradation diminished the amount of Ku70 associated with gamma-H2AX but not that of NDH II. In vitro binding studies with recombinant NDH II and H2AX phosphorylated by DNA-dependent protein kinase confirmed a direct physical interaction between NDH II and gamma-H2AX. Thereby, the NDH II DEXH domain alone, i.e. its catalytic core, was able to support binding to gamma-H2AX. Congruently, after actinomycin D treatment, NDH II accumulated in RNA-containing nuclear bodies that predominantly co-localized with gamma-H2AX foci. Taken together, these results suggest that histone gamma-H2AX promotes binding of NDH II to transcriptionally stalled sites on chromosomal DNA."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411444200"xsd:string
http://purl.uniprot.org/citations/15613478http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m411444200"xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Zhang S."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Grosse F."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Grosse F."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Hemmerich P."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Hemmerich P."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Mischo H.E."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/author"Mischo H.E."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/pages"9586-9594"xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/pages"9586-9594"xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/title"Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/title"Actinomycin D induces histone gamma-H2AX foci and complex formation of gamma-H2AX with Ku70 and nuclear DNA helicase II."xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15613478http://purl.uniprot.org/core/volume"280"xsd:string
http://purl.uniprot.org/citations/15613478http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15613478
http://purl.uniprot.org/citations/15613478http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15613478