ArticleOpen biology2016
Structural and biochemical analyses of monoubiquitinated human histones H2B and H4.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 41 citations in OpenAlex.
- LDOC1 connects histone H2B monoubiquitination to tumor cell plasticity in non-small cell lung cancer.Cell communication and signaling : CCS · 2026Article
- Nucleosomes represent a crucial target for the intra-S phase checkpoint in response to replication stress.Science advances · 2025Article
- Ubiquitinated histone H2B as gatekeeper of the nucleosome acidic patch.Nucleic acids research · 2024Article
- Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024Review
- The Effects of Histone H2B Ubiquitylations on the Nucleosome Structure and Internucleosomal Interactions.Biochemistry · 2022Article
- Histone Modifications, Internucleosome Dynamics, and DNA Stresses: How They Cooperate to "Functionalize" Nucleosomes.Frontiers in genetics · 2022Article
- Ubiquitin-Specific Proteases: Players in Cancer Cellular Processes.Pharmaceuticals (Basel, Switzerland) · 2021Review
- Chromatin Regulation through Ubiquitin and Ubiquitin-like Histone Modifications.Trends in biochemical sciences · 2021Review
- ReducedCancers · 2021Article
- Ubiquitin chromatin remodelling after DNA damage is associated with the expression of key cancer genes and pathways.Cellular and molecular life sciences : CMLS · 2021Article
- A non-canonical monovalent zinc finger stabilizes the integration of Cfp1 into the H3K4 methyltransferase complex COMPASS.Nucleic acids research · 2020Article
- Writing Histone Monoubiquitination in Human Malignancy-The Role of RING Finger E3 Ubiquitin Ligases.Genes · 2019Review
- Effects of histone H2B ubiquitylation on the nucleosome structure and dynamics.Nucleic acids research · 2018Article
- Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome.eLife · 2018Article
- The interplay of histone H2B ubiquitination with budding and fission yeast heterochromatin.Current genetics · 2018Review
- A systematic analysis of nucleosome core particle and nucleosome-nucleosome stacking structure.Scientific reports · 2018Article
- Cryo-electron microscopy of chromatin biology.Acta crystallographica. Section D, Structural biology · 2017Review
- Ubiquitin utilizes an acidic surface patch to alter chromatin structure.Nature chemical biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Monoubiquitination is a major histone post-translational modification. In humans, the histone H2B K120 and histone H4 K31 residues are monoubiquitinated and may form transcriptionally active chromatin. In this study, we reconstituted nucleosomes containing H2B monoubiquitinated at position 120 (H2Bub120) and/or H4 monoubiquitinated at position 31 (H4ub31). We found that the H2Bub120 and H4ub31 monoubiquitinations differently affect nucleosome stability: the H2Bub120 monoubiquitination enhances the H2A-H2B association with the nucleosome, while the H4ub31 monoubiquitination decreases the H3-H4 stability in the nucleosome, when compared with the unmodified nucleosome. The H2Bub120 and H4ub31 monoubiquitinations both antagonize the Mg(2+)-dependent compaction of a poly-nucleosome, suggesting that these monoubiquitinations maintain more relaxed conformations of chromatin. In the crystal structure, the H2Bub120 and H4ub31 monoubiquitinations do not change the structure of the nucleosome core particle and the ubiquitin molecules were flexibly disordered in the H2Bub120/H4ub31 nucleosome structure. These results revealed the differences and similarities of the H2Bub120 and H4ub31 monoubiquitinations at the mono- and poly-nucleosome levels and provide novel information to clarify the roles of monoubiquitination in chromatin.
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