ArticleeLife2021
Sumoylation of the human histone H4 tail inhibits p300-mediated transcription by RNA polymerase II in cellular extracts.
Article in eLife, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Chemical biology tools for studying histone post-translational modifications.Cell chemical biology · 2026Review
- Transient SUMOylation inhibition in human pre-adipocytes stably imprints a transcriptional beiging fate.Nucleic acids research · 2026Article
- SUMOylation is destined for regulatory T cell-related immune dysregulation.Cell death discovery · 2026Review
- Zmiz1-Mediated SUMOylation of NLRP3 Inflammasome Regulates Satellite Glial Cell Activation and Neuronal Autophagy in Trigeminal Neuralgia.Inflammation · 2025Article
- PLAMseq enables the proteo-genomic characterization of chromatin-associated proteins and protein interactions in a single workflow.Science advances · 2025Article
- piRNA gene density and SUMOylation organize piRNA transcriptional condensate formation.Nature structural & molecular biology · 2025Article
- Histone modifications and metabolic reprogramming in tumor-associated macrophages: a potential target of tumor immunotherapy.Frontiers in immunology · 2025Review
- Particulate matter-induced epigenetic modifications and lung complications.European respiratory review : an official journal of the European Respiratory Society · 2024Review
- Crosstalk between SUMOylation and other post-translational modifications in breast cancer.Cellular & molecular biology letters · 2024Review
- Asprosin: its function as a novel endocrine factor in metabolic-related diseases.Journal of endocrinological investigation · 2024Review
- Potential Signature Therapeutic Biomarkers TOP2A, MAD2L1, and CDK1 in Colorectal Cancer: A Systems Biomedicine-Based Approach.Biochemical genetics · 2024Article
- Substrate and Functional Diversity of Protein Lysine Post-translational Modifications.Genomics, proteomics & bioinformatics · 2024Review
- An Overview of the Epigenetic Modifications in the Brain under Normal and Pathological Conditions.International journal of molecular sciences · 2024Review
- Covalent hitchhikers guide proteins to the nucleus.Cell chemical biology · 2024Article
- Gastric Cancer in the Era of Epigenetics.International journal of molecular sciences · 2024Review
- Cyclic AMP induces reversible EPAC1 condensates that regulate histone transcription.Nature communications · 2023Article
- The semisynthesis of site-specifically modified histones and histone-based probes of chromatin-modifying enzymes.Methods (San Diego, Calif.) · 2023Article
- Total chemical synthesis of sumoylated histone H4 reveals negative biochemical crosstalk with histone ubiquitylation.Chemical communications (Cambridge, England) · 2023Article
- The roles of histone modifications in tumorigenesis and associated inhibitors in cancer therapy.Journal of the National Cancer Center · 2022Review
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
Abstract
The post-translational modification of histones by the small ubiquitin-like modifier (SUMO) protein has been associated with gene regulation, centromeric localization, and double-strand break repair in eukaryotes. Although sumoylation of histone H4 was specifically associated with gene repression, this could not be proven due to the challenge of site-specifically sumoylating H4 in cells. Biochemical crosstalk between SUMO and other histone modifications, such as H4 acetylation and H3 methylation, that are associated with active genes also remains unclear. We addressed these challenges in mechanistic studies using an H4 chemically modified at Lys12 by SUMO-3 (H4K12su) and incorporated into mononucleosomes and chromatinized plasmids for functional studies. Mononucleosome-based assays revealed that H4K12su inhibits transcription-activating H4 tail acetylation by the histone acetyltransferase p300, as well as transcription-associated H3K4 methylation by the extended catalytic module of the Set1/COMPASS (complex of proteins associated with Set1) histone methyltransferase complex. Activator- and p300-dependent in vitro transcription assays with chromatinized plasmids revealed that H4K12su inhibits both H4 tail acetylation and RNA polymerase II-mediated transcription. Finally, cell-based assays with a SUMO-H4 fusion that mimics H4 tail sumoylation confirmed the negative crosstalk between histone sumoylation and acetylation/methylation. Thus, our studies establish the key role for histone sumoylation in gene silencing and its negative biochemical crosstalk with active transcription-associated marks in human cells.
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