ArticleBiochemistry2012
Identification of an ubinuclein 1 region required for stability and function of the human HIRA/UBN1/CABIN1/ASF1a histone H3.3 chaperone complex.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 39 citations in OpenAlex.
- APC coordinates GSK3 phosphorylation of SETD8 to suppress colorectal cancer.Cell reports · 2026Article
- Histone H3 availability is more important for development than H3.2 versus H3.3 subtype identity.bioRxiv : the preprint server for biology · 2026Article
- Ubinuclein 2 is essential for mouse development and functions in X chromosome inactivation.PLoS genetics · 2025Article
- The Hira complex regulates Gli3R-dependent transcription in Hedgehog signaling and medulloblastoma cell growth and migration.Scientific reports · 2025Article
- Structure of the Hir histone chaperone complex.Molecular cell · 2024Article
- The Histone Chaperone Network Is Highly Conserved inInternational journal of molecular sciences · 2023Article
- HIRA complex presets transcriptional potential through coordinating depositions of the histone variants H3.3 and H2A.Z on the poised genes in mESCs.Nucleic acids research · 2022Article
- PML nuclear bodies and chromatin dynamics: catch me if you can!Nucleic acids research · 2020Review
- ZO-2 Is a Master Regulator of Gene Expression, Cell Proliferation, Cytoarchitecture, and Cell Size.International journal of molecular sciences · 2019Review
- The HIRA histone chaperone complex subunit UBN1 harbors H3/H4- and DNA-binding activity.The Journal of biological chemistry · 2019Article
- Promyelocytic leukemia (PML) nuclear bodies (NBs) induce latent/quiescent HSV-1 genomes chromatinization through a PML NB/Histone H3.3/H3.3 Chaperone Axis.PLoS pathogens · 2018Article
- Functional activity of the H3.3 histone chaperone complex HIRA requires trimerization of the HIRA subunit.Nature communications · 2018Article
- Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Journal of molecular biology · 2017Review
- The Histone Variant H3.3 in Transcriptional Regulation and Human Disease.Journal of molecular biology · 2017Review
- A Molecular Prospective for HIRA Complex Assembly and H3.3-Specific Histone Chaperone Function.Journal of molecular biology · 2017Review
- H3.Y discriminates between HIRA and DAXX chaperone complexes and reveals unexpected insights into human DAXX-H3.3-H4 binding and deposition requirements.Nucleic acids research · 2017Article
- DNA copy number alterations, gene expression changes and disease-free survival in patients with colorectal cancer: a 10 year follow-up.Cellular oncology (Dordrecht, Netherlands) · 2016Article
- O-linked N-acetylglucosamine transferase (OGT) interacts with the histone chaperone HIRA complex and regulates nucleosome assembly and cellular senescence.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Identification of a Novel Coregulator, SH3YL1, That Interacts With the Androgen Receptor N-Terminus.Molecular endocrinology (Baltimore, Md.) · 2015Article
- Ubinuclein-1 confers histone H3.3-specific-binding by the HIRA histone chaperone complex.Nature communications · 2015Article
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9 authors at 2 institutions in 1 country.
Funding
Abstract
The mammalian HIRA/UBN1/CABIN1/ASF1a (HUCA) histone chaperone complex deposits the histone H3 variant H3.3 into chromatin and is linked to gene activation, repression, and chromatin assembly in diverse cell contexts. We recently reported that a short N-terminal fragment of UBN1 containing amino acids 1-175 is necessary and sufficient for interaction with the WD repeats of HIRA and attributed this interaction to a region from residues 120-175 that is highly conserved with the yeast ortholog Hpc2 and so termed the HRD for Hpc2-related domain. In this report, through a more comprehensive and refined biochemical and mutational analysis, we identify a smaller and more moderately conserved region within residues 41-77 of UBN1, which we term the NHRD, that is essential for interaction with the HIRA WD repeats; we further demonstrate that the HRD is dispensable for this interaction. We employ analytical ultracentrifugation studies to demonstrate that the NHRD of UBN1 and the WD repeats of HIRA form a tight 1:1 complex with a dissociation constant in the nanomolar range. Mutagenesis experiments identify several key residues in the NHRD that are required for interaction with the HIRA WD repeat domain, stability of the HUCA complex in vitro and in vivo, and changes in chromatin organization in primary human cells. Together, these studies implicate the NHRD domain of UBN1 as being an essential region for HIRA interaction and chromatin organization by the HUCA complex.
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