{"doi":"10.1101/2023.05.09.540004","title":"Spontaneous Histone Exchange Between Nucleosomes","abstract":"<jats:title>ABSTRACT</jats:title>\n                <jats:p>\n                  The nucleosome is the fundamental gene-packing unit in eukaryotes. Nucleosomes comprise ∼147 bp DNA wrapped around an octameric histone protein core composed of two H2A-H2B dimers and one (H3-H4)\n                  <jats:sub>2</jats:sub>\n                  tetramer. The strong yet flexible DNA-histone interactions are a physical basis of the dynamic regulation of genes packaged in chromatin. The dynamic nature of DNA-histone interactions implies that nucleosomes dissociate DNA-histone contacts transiently and repeatedly. This kinetic instability may lead to spontaneous nucleosome disassembly or histone exchange between nucleosomes. At a high nucleosome concentration, nucleosome-nucleosome collisions and subsequent histone exchange would be a more likely pathway, where nucleosomes act as their own histone chaperone. The spontaneous histone exchange would serve as a mechanism for maintaining the overall chromatin stability although it has never been reported. We employed three-color single-molecule FRET (smFRET) to demonstrate that histone H2A-H2B dimers are exchanged spontaneously between nucleosomes and that the time scale is on a few tens of seconds at a physiological nucleosome concentration. The rate of histone exchange increases at a higher monovalent salt concentration, with histone acetylated nucleosomes, and in the presence of histone chaperone Nap1, while it remains unchanged at a higher temperature, and decreases upon DNA methylation. These results support histone exchange via transient and repetitive partial disassembly of the nucleosome and corroborate spontaneous histone diffusion in a compact chromatin context, modulating the local concentrations of histone modifications and variants.\n                </jats:p>","journal":"bioRxiv (Cold Spring Harbor Laboratory)","year":null,"id":13757,"datarank":0.246321801431788,"base_score":1.3862943611198906,"endowment":1.3862943611198906,"self_citation_contribution":0.20794415416798362,"citation_network_contribution":0.038377647263804375,"self_endowment_contribution":0.20794415416798362,"citer_contribution":0.038377647263804375,"corpus_percentile":null,"corpus_rank":null,"citation_count":3,"citer_count":3,"citers_with_citation_signal":3,"citers_with_endowment":3,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":111469,"name":"Mai Thao Huynh","orcid":null,"position":1,"is_corresponding":false},{"id":44963,"name":"Tae-Hee Lee","orcid":"0000-0003-2034-6394","position":2,"is_corresponding":false},{"id":111468,"name":"Subhra Kanti Das","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"base_score":1.3862943611198906,"endowment":1.3862943611198906,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"37215040","pmcid":null,"openalex_id":"https://openalex.org/W4376280143","authors":[],"funders":[{"funder_name":"National Institutes of Health","grant_id":"5R01GM123164-04","title":"Dynamics of histone-DNA interaction"},{"funder_name":"National Institutes of Health","grant_id":"5R01GM130793-02","title":"Effects of histone ubiquitylation on nucleosome dynamics"},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM123164","title":null},{"funder_name":"NIGMS NIH HHS","grant_id":"R01 GM130793","title":null}],"total_grants":4,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[{"year":2024,"count":1},{"year":2025,"count":2}],"oa_status":"green","license":"CC BY","oa_locations":[{"url":"https://www.biorxiv.org/content/biorxiv/early/2023/05/11/2023.05.09.540004.full.pdf","host_type":"repository"},{"url":"http://www.jbc.org/article/S0021925823020653/pdf","host_type":"GREEN"},{"url":"https://www.biorxiv.org/content/biorxiv/early/2023/05/11/2023.05.09.540004.full.pdf","host_type":"repository"},{"url":"https://syndication.highwire.org/content/doi/10.1101/2023.05.09.540004","host_type":"publisher"},{"url":"https://doi.org/10.1101/2023.05.09.540004","host_type":"repository"},{"url":"https://pubmed.ncbi.nlm.nih.gov/37215040","host_type":"repository"},{"url":"https://www.ncbi.nlm.nih.gov/pmc/articles/10197660","host_type":"repository"},{"url":"https://doi.org/10.1016/j.jbc.2023.105037","host_type":""},{"url":"https://pubmed.ncbi.nlm.nih.gov/37442235","host_type":""},{"url":"http://dx.doi.org/10.1016/j.jbc.2023.105037","host_type":""}],"fields_of_study":["Genomics and Chromatin Dynamics","DNA and Nucleic Acid Chemistry","Epigenetics and DNA Methylation","Biology","Medicine"],"mesh_terms":[],"keywords":["Nucleosome","Histone octamer","Histone methylation","Histone code","Histone H1","Chromatosome","Histone","Linker DNA","Histone H2A","Histone methyltransferase","Cell biology","Chemistry","Biology","Biophysics","Genetics","DNA","DNA methylation","Gene expression","Gene","Histones","Histone Chaperones","Chromatin","Research Article","Nucleosomes"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-05-31T15:21:33.543799Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}