ArticleThe EMBO journal2019
The Ulp2 SUMO protease promotes transcription elongation through regulation of histone sumoylation.
Article in The EMBO journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 39 citations in OpenAlex.
- Organelle regulation of SUMOylation: regulatory mechanisms and therapeutic application.Journal of advanced research · 2026Review
- Sumoylation of cyclin and its therapeutic potential for cancer.Animal cells and systems · 2026Review
- Auto-sumoylation of the yeast Ubc9 E2 SUMO-conjugating enzyme extends cellular lifespan.Nature communications · 2025Article
- Histone H3 lysine 9 tri-methylation is associated with pterygium.BMC ophthalmology · 2025Article
- The SUMO Pathway.Methods in molecular biology (Clifton, N.J.) · 2025Review
- Histone Modification Pathways Suppressing Cryptic Transcription.Epigenomes · 2024Article
- Article
- Yeast Small Ubiquitin-Like Modifier (SUMO) Protease Ulp2 is Involved in RNA Splicing.Development & reproduction · 2024Article
- Histone H2B ubiquitylation: Connections to transcription and effects on chromatin structure.Biochimica et biophysica acta. Gene regulatory mechanisms · 2024Review
- DeSUMOylation of a Verticillium dahliae enolase facilitates virulence by derepressing the expression of the effector VdSCP8.Nature communications · 2023Article
- The semisynthesis of site-specifically modified histones and histone-based probes of chromatin-modifying enzymes.Methods (San Diego, Calif.) · 2023Article
- Function and regulation of ubiquitin-like SUMO system in heart.Frontiers in cell and developmental biology · 2023Review
- Histone modification inComputational and structural biotechnology journal · 2023Review
- SUMO pathway is required for ribosome biogenesis.BMB reports · 2022Review
- SUMOylation targeting mitophagy in cardiovascular diseases.Journal of molecular medicine (Berlin, Germany) · 2022Review
- SUMOylation and Major Depressive Disorder.International journal of molecular sciences · 2022Review
- A versatile new tool derived from a bacterial deubiquitylase to detect and purify ubiquitylated substrates and their interacting proteins.PLoS biology · 2022Article
- Nuclear mRNA Export and Aging.International journal of molecular sciences · 2022Review
- Post-Translational Modifications of Histones Are Versatile Regulators of Fungal Development and Secondary Metabolism.Toxins · 2022Review
- Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Many eukaryotic proteins are regulated by modification with the ubiquitin-like protein small ubiquitin-like modifier (SUMO). This linkage is reversed by SUMO proteases, of which there are two in Saccharomyces cerevisiae, Ulp1 and Ulp2. SUMO-protein conjugation regulates transcription, but the roles of SUMO proteases in transcription remain unclear. We report that Ulp2 is recruited to transcriptionally active genes to control local polysumoylation. Mutant ulp2 cells show impaired association of RNA polymerase II (RNAPII) with, and diminished expression of, constitutively active genes and the inducible CUP1 gene. Ulp2 loss sensitizes cells to 6-azauracil, a hallmark of transcriptional elongation defects. We also describe a novel chromatin regulatory mechanism whereby histone-H2B ubiquitylation stimulates histone sumoylation, which in turn appears to inhibit nucleosome association of the Ctk1 kinase. Ctk1 phosphorylates serine-2 (S2) in the RNAPII C-terminal domain (CTD) and promotes transcript elongation. Removal of both ubiquitin and SUMO from histones is needed to overcome the impediment to S2 phosphorylation. These results suggest sequential ubiquitin-histone and SUMO-histone modifications recruit Ulp2, which removes polySUMO chains and promotes RNAPII transcription elongation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.