{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["16(1)"],"submitter":["Benhamza I"],"pubmed_abstract":["Using an in situ nucleosome stability assay based on salt extraction, we identified distinct stability features of H2A.Z-containing nucleosomes linked to alternative interactions of the histone variant's C-terminal tail (Imre et al., Nat. Commun., 2024). In DT40 cells expressing either full-length or C-terminally truncated human H2A.Z1, we show that nucleosome stability is tail-dependent also through the spectacles of intercalator sensitivity, raising the possibility that the tail may bind to DNA in a superhelicity-dependent fashion. Supporting this, fluorescence correlation spectroscopy detected binding of a fluorescent H2A.Z-tail nonapeptide to supercoiled-but not relaxed-plasmid DNA, while a scrambled peptide showed negligible binding. The DNA topology-dependent binding of the unstructu"],"journal":["Nucleus (Austin, Tex.)"],"pagination":["2557113"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12427435"],"repository":["biostudies-literature"],"pubmed_title":["H2A.Z-nucleosomes are stabilized by the superhelicity-dependent DNA binding of the C-terminal tail of the histone variant."],"pmcid":["PMC12427435"],"pubmed_authors":["Goda K","Imre L","Nanasi P","Szabo G","Enyedi KN","Vamosi G","Yu Z","Sen P","Benhamza I"],"additional_accession":[]},"is_claimable":false,"name":"H2A.Z-nucleosomes are stabilized by the superhelicity-dependent DNA binding of the C-terminal tail of the histone variant.","description":"Using an in situ nucleosome stability assay based on salt extraction, we identified distinct stability features of H2A.Z-containing nucleosomes linked to alternative interactions of the histone variant's C-terminal tail (Imre et al., Nat. Commun., 2024). In DT40 cells expressing either full-length or C-terminally truncated human H2A.Z1, we show that nucleosome stability is tail-dependent also through the spectacles of intercalator sensitivity, raising the possibility that the tail may bind to DNA in a superhelicity-dependent fashion. Supporting this, fluorescence correlation spectroscopy detected binding of a fluorescent H2A.Z-tail nonapeptide to supercoiled-but not relaxed-plasmid DNA, while a scrambled peptide showed negligible binding. The DNA topology-dependent binding of the unstructu","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Dec","modification":"2026-06-01T12:04:37.943Z","creation":"2026-04-08T12:01:59.623Z"},"accession":"S-EPMC12427435","cross_references":{"pubmed":["40926315"],"doi":["10.1080/19491034.2025.2557113"]}}