ArticleProceedings of the National Academy of Sciences of the United States of America2008
Modulation of RNA polymerase II subunit composition by ubiquitylation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
32 citing papers in PubMed, 64 citations in OpenAlex.
- CTDP1 and RPB7 stabilize Pol II and permit reinitiation.Nature communications · 2025Article
- Multiple Forms and Functions of Premature Termination by RNA Polymerase II.Journal of molecular biology · 2025Review
- Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024Review
- ARMC5 controls the degradation of most Pol II subunits, and ARMC5 mutation increases neural tube defect risks in mice and humans.Genome biology · 2024Article
- Never a dull enzyme, RNA polymerase II.Transcription · 2023Review
- Article
- Protein Homeostasis Networks and the Use of Yeast to Guide Interventions in Alzheimer's Disease.International journal of molecular sciences · 2020Review
- Ubiquitin-proteasome-mediated cyclin C degradation promotes cell survival following nitrogen starvation.Molecular biology of the cell · 2020Article
- Article
- Substrate selection by the proteasome through initiation regions.Protein science : a publication of the Protein Society · 2019Review
- Ccr4-Not maintains genomic integrity by controlling the ubiquitylation and degradation of arrested RNAPII.Genes & development · 2019Article
- Methods review: Mass spectrometry analysis of RNAPII complexes.Methods (San Diego, Calif.) · 2019Review
- Creation of Individual Scientific Concept-Centered Semantic Maps Based on Automated Text-Mining Analysis of PubMed.Advances in bioinformatics · 2018Article
- Human p53 interacts with the elongating RNAPII complex and is required for the release of actinomycin D induced transcription blockage.Scientific reports · 2017Article
- Interaction of Gcn4 with target gene chromatin is modulated by proteasome function.Molecular biology of the cell · 2016Article
- Touch and go: nuclear proteolysis in the regulation of metabolic genes and cancer.FEBS letters · 2016Review
- Antagonistic roles for the ubiquitin ligase Asr1 and the ubiquitin-specific protease Ubp3 in subtelomeric gene silencing.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Using both strands: The fundamental nature of antisense transcription.Bioarchitecture · 2016Article
- Molecular mechanisms of gonadotropin-releasing hormone signaling: integrating cyclic nucleotides into the network.Frontiers in endocrinology · 2013Review
- Correct assembly of RNA polymerase II depends on the foot domain and is required for multiple steps of transcription in Saccharomyces cerevisiae.Molecular and cellular biology · 2013Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Emerging evidence suggests that components of the ubiquitin-proteasome system are involved in the regulation of gene expression. A variety of factors, including transcriptional activators, coactivators, and histones, are controlled by ubiquitylation, but the mechanisms through which this modification can function in transcription are generally unknown. Here, we report that the Saccharomyces cerevisiae protein Asr1 is a RING finger ubiquitin-ligase that binds directly to RNA polymerase II via the carboxyl-terminal domain (CTD) of the largest subunit of the enzyme. We show that interaction of Asr1 with the CTD depends on serine-5 phosphorylation within the CTD and results in ubiquitylation of at least 2 subunits of the enzyme, Rpb1 and Rpb2. Ubiquitylation by Asr1 leads to the ejection of the Rpb4/Rpb7 heterodimer from the polymerase complex and is associated with inactivation of polymerase function. Our data demonstrate that ubiquitylation can directly alter the subunit composition of a core component of the transcriptional machinery and provide a paradigm for how ubiquitin can influence gene activity.
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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.