ArticleThe Journal of biological chemistry2019
The HIRA histone chaperone complex subunit UBN1 harbors H3/H4- and DNA-binding activity.
Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- Structure of the human HIRA histone chaperone with a nucleosome suggests a stepwise nucleosome assembly mechanism.bioRxiv : the preprint server for biology · 2026Article
- HIRA defines early replication initiation zones independently of their genome compartment.Nature communications · 2025Article
- Daxx and HIRA go viral - How chromatin remodeling complexes affect DNA virus infection.Tumour virus research · 2025Review
- The Hira complex regulates Gli3R-dependent transcription in Hedgehog signaling and medulloblastoma cell growth and migration.Scientific reports · 2025Article
- Article
- Histone chaperone HIRA, promyelocytic leukemia protein, and p62/SQSTM1 coordinate to regulate inflammation during cell senescence.Molecular cell · 2024Article
- Review
- Structure of the Hir histone chaperone complex.Molecular cell · 2024Article
- HIRA vs. DAXX: the two axes shaping the histone H3.3 landscape.Experimental & molecular medicine · 2024Review
- Unraveling the immunogenetic landscape of autism spectrum disorder: a comprehensive bioinformatics approach.Frontiers in immunology · 2024Article
- Understanding copy number variations through their genes: a molecular view on 16p11.2 deletion and duplication syndromes.Frontiers in pharmacology · 2024Review
- The cell-cycle choreography of H3 variants shapes the genome.Molecular cell · 2023Review
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- Two HIRA-dependent pathways mediate H3.3 de novo deposition and recycling during transcription.Nature structural & molecular biology · 2020Article
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Authors and funding
9 authors at 4 institutions in 1 country.
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Abstract
The HIRA histone chaperone complex is composed of the proteins HIRA, UBN1, and CABIN1 and cooperates with the histone chaperone ASF1a to specifically bind and deposit H3.3/H4 into chromatin. We recently reported that the UBN1 Hpc2-related domain (HRD) specifically binds to H3.3/H4 over H3.1/H4. However, the mechanism for HIRA complex deposition of H3.3/H4 into nucleosomes remains unclear. Here, we characterize a central region of UBN1 (UBN1 middle domain) that is evolutionarily conserved and predicted to have helical secondary structure. We report that the UBN1 middle domain has dimer formation activity and binds to H3/H4 in a manner that does not discriminate between H3.1 and H3.3. We additionally identify a nearby DNA-binding domain in UBN1, located between the UBN1 HRD and middle domain, which binds DNA through electrostatic contacts involving several conserved lysine residues. Together, these observations suggest a mechanism for HIRA-mediated H3.3/H4 deposition whereby UBN1 associates with DNA and dimerizes to mediate formation of an (H3.3/H4)
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