ArticleProceedings of the National Academy of Sciences of the United States of America2009
Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 98 papers.
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98 citing papers in PubMed.
- Systemic degradation of repressive transcription factors gates gene expression and cell fate specification.bioRxiv : the preprint server for biology · 2026Article
- K63-linked ubiquitylation of S2P-RNAPII regulates transcription in a DNAPK inter-dependent manner in response to double-strand breaks.Nucleic acids research · 2026Article
- A testis-specific E3 ubiquitin ligase complex governs spermiogenesis and male fertility.Nature communications · 2026Article
- Transcription-coupled repair: tangled up in convoluted repair.The FEBS journal · 2025Review
- Review
- TRIP12's role in the governance of DNA polymerase β involvement in DNA damage response and repair.Nucleic acids research · 2025Article
- Stalled disomes marked by Hel2-dependent ubiquitin chains undergo Ubp2/Ubp3-mediated deubiquitination upon translational run-off.Communications biology · 2025Article
- Differential processing of RNA polymerase II at DNA damage correlates with transcription-coupled repair syndrome severity.Nucleic acids research · 2024Article
- DNA break induces rapid transcription repression mediated by proteasome-dependent RNAPII removal.Cell reports · 2024Article
- Proteasome Inhibition Reprograms Chromatin Landscape in Breast Cancer.Cancer research communications · 2024Article
- Ubiquiton-An inducible, linkage-specific polyubiquitylation tool.Molecular cell · 2024Article
- ARMC5 controls the degradation of most Pol II subunits, and ARMC5 mutation increases neural tube defect risks in mice and humans.Genome biology · 2024Article
- Structure of the transcribing RNA polymerase II-Elongin complex.Nature structural & molecular biology · 2023Article
- New roles for elongation factors in RNA polymerase II ubiquitylation and degradation.Biochimica et biophysica acta. Gene regulatory mechanisms · 2023Review
- RNAPII response to transcription-blocking DNA lesions in mammalian cells.The FEBS journal · 2023Review
- RNAPII Degradation Factor Def1 Is Required for Development, Stress Response, and Full Virulence ofJournal of fungi (Basel, Switzerland) · 2023Article
- NEIL3-mediated proteasomal degradation facilitates the repair of cisplatin-induced DNA damage in human cells.Scientific reports · 2023Article
- Regulation of RNA Polymerase I Stability and Function.Cancers · 2022Review
- Review
- Yeast Smy2 and its human homologs GIGYF1 and -2 regulate Cdc48/VCP function during transcription stress.Cell reports · 2022Article
38 more citing papers are in PubMed but not listed here.
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11 authors.
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Abstract
The proteasome degrades proteins modified by polyubiquitylation, so correctly controlled ubiquitylation is crucial to avoid unscheduled proteolysis of essential proteins. The mechanism regulating proteolysis of RNAPII has been controversial since two distinct ubiquitin ligases (E3s), Rsp5 (and its human homologue NEDD4) and Elongin-Cullin complex, have both been shown to be required for its DNA-damage-induced polyubiquitylation. Here we show that these E3s work sequentially in a two-step mechanism. First, Rsp5 adds mono-ubiquitin, or sometimes a ubiquitin chain linked via ubiquitin lysine 63 that does not trigger proteolysis. When produced, the K63 chain can be trimmed to mono-ubiquitylation by an Rsp5-associated ubiquitin protease, Ubp2. Based on this mono-ubiquitin moiety on RNAPII, an Elc1/Cul3 complex then produces a ubiquitin chain linked via lysine 48, which can trigger proteolysis. Likewise, for correct polyubiquitylation of human RNAPII, NEDD4 cooperates with the ElonginA/B/C-Cullin 5 complex. These data indicate that RNAPII polyubiquitylation requires cooperation between distinct, sequentially acting ubiquitin ligases, and raise the intriguing possibility that other members of the large and functionally diverse family of NEDD4-like ubiquitin ligases also require the assistance of a second E3 when targeting proteins for degradation.
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