| http://purl.uniprot.org/citations/23075851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23075851 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23075851 | http://www.w3.org/2000/01/rdf-schema#comment | "Histone chaperones represent a structurally and functionally diverse family of histone-binding proteins that prevent promiscuous interactions of histones before their assembly into chromatin. DAXX is a metazoan histone chaperone specific to the evolutionarily conserved histone variant H3.3. Here we report the crystal structures of the DAXX histone-binding domain with a histone H3.3-H4 dimer, including mutants within DAXX and H3.3, together with in vitro and in vivo functional studies that elucidate the principles underlying H3.3 recognition specificity. Occupying 40% of the histone surface-accessible area, DAXX wraps around the H3.3-H4 dimer, with complex formation accompanied by structural transitions in the H3.3-H4 histone fold. DAXX uses an extended α-helical conformation to compete with major inter-histone, DNA and ASF1 interaction sites. Our structural studies identify recognition elements that read out H3.3-specific residues, and functional studies address the contributions of Gly 90 in H3.3 and Glu 225 in DAXX to chaperone-mediated H3.3 variant recognition specificity."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature11608"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.org/dc/terms/identifier | "doi:10.1038/nature11608"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Huang H."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Huang H."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Patel D.J."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Patel D.J."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Allis C.D."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Allis C.D."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Chin J.W."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Chin J.W."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Lewis P.W."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Lewis P.W."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Elsasser S.J."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/author | "Elsasser S.J."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/date | "2012"xsd:gYear |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/pages | "560-565"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/pages | "560-565"xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/title | "DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition."xsd:string |
| http://purl.uniprot.org/citations/23075851 | http://purl.uniprot.org/core/title | "DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition."xsd:string |