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http://purl.uniprot.org/citations/28320872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28320872http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/28320872http://www.w3.org/2000/01/rdf-schema#comment"Histone variants are nonallelic isoforms of canonical histones, and they are deposited, in contrast to canonical histones, in a replication-independent (RI) manner. RI deposition of H3.3, a histone variant from the H3.3 family, is mediated in mammals by distinct pathways involving either the histone regulator A (HIRA) complex or the death-associated protein (DAXX)/α-thalassemia X-linked mental retardation protein (ATRX) complex. Here, we investigated the function of the Drosophila DAXX-like protein (DLP) by using both fly genetic approaches and protein biochemistry. DLP specifically interacts with H3.3 and shows a prominent localization on the base of the X chromosome, where it appears to act in concert with XNP, the Drosophila homolog of ATRX, in heterochromatin assembly and maintenance. The functional association between DLP and XNP is further supported by a series of experiments that illustrate genetic interactions and the DLP-XNP-dependent localization of specific chromosomal proteins. In addition, DLP both participates in the RI deposition of H3.3 and associates with anti-silencing factor 1 (ASF1). We suggest, in agreement with a recently proposed model, that DLP and ASF1 are part of a predeposition complex, which is recruited by XNP and is necessary to prevent DNA exposure in the nucleus."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00597-16"xsd:string
http://purl.uniprot.org/citations/28320872http://purl.org/dc/terms/identifier"doi:10.1128/mcb.00597-16"xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Hamiche A."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Hamiche A."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Fromental-Ramain C."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Fromental-Ramain C."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Ramain P."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/author"Ramain P."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/date"2017"xsd:gYear
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/name"Mol. Cell. Biol."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/title"The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/title"The Drosophila DAXX-Like Protein (DLP) Cooperates with ASF1 for H3.3 Deposition and Heterochromatin Formation."xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/28320872http://purl.uniprot.org/core/volume"37"xsd:string
http://purl.uniprot.org/citations/28320872http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28320872
http://purl.uniprot.org/citations/28320872http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/28320872
http://purl.uniprot.org/citations/28320872http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28320872
http://purl.uniprot.org/citations/28320872http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/28320872
http://purl.uniprot.org/uniprot/Q9VMD0http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/28320872
http://purl.uniprot.org/uniprot/Q9V464http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/28320872