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http://purl.uniprot.org/citations/34819355http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34819355http://www.w3.org/2000/01/rdf-schema#comment"Chromosomal duplication requires de novo assembly of nucleosomes from newly synthesized histones, and the process involves a dynamic network of interactions between histones and histone chaperones. sNASP and ASF1 are two major histone H3-H4 chaperones found in distinct and common complexes, yet how sNASP binds H3-H4 in the presence and absence of ASF1 remains unclear. Here we show that, in the presence of ASF1, sNASP principally recognizes a partially unfolded Nα region of histone H3, and in the absence of ASF1, an additional sNASP binding site becomes available in the core domain of the H3-H4 complex. Our study also implicates a critical role of the C-terminal tail of H4 in the transfer of H3-H4 between sNASP and ASF1 and the coiled-coil domain of sNASP in nucleosome assembly. These findings provide mechanistic insights into coordinated histone binding and transfer by histone chaperones."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.org/dc/terms/identifier"doi:10.1101/gad.349100.121"xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Chen J."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Jin W."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Hu J."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Li G."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Wang M."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Liu C.P."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/author"Xu R.M."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/name"Genes Dev"xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/pages"1610-1624"xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/title"Distinct histone H3-H4 binding modes of sNASP reveal the basis for cooperation and competition of histone chaperones."xsd:string
http://purl.uniprot.org/citations/34819355http://purl.uniprot.org/core/volume"35"xsd:string
http://purl.uniprot.org/citations/34819355http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34819355
http://purl.uniprot.org/citations/34819355http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34819355
http://purl.uniprot.org/uniprot/#_P62805-mappedCitation-34819355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/#_P68431-mappedCitation-34819355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/#_P49321-mappedCitation-34819355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/#_Q9Y294-mappedCitation-34819355http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/P62805http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/Q9Y294http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/P68431http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34819355
http://purl.uniprot.org/uniprot/P49321http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34819355