ArticleThe Journal of biological chemistry2009
Rpb9 subunit controls transcription fidelity by delaying NTP sequestration in RNA polymerase II.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- Widespread epistasis shapes RNA polymerase II active site function and evolution.Nature communications · 2025Article
- The hidden costs of imperfection: transcription errors in protein aggregation diseases.Current opinion in genetics & development · 2025Review
- A mobile genetic element-derived primase-polymerase harbors multiple activities implicated in DNA replication and repair.Nucleic acids research · 2025Article
- RNA Polymerase II Activity Control of Gene Expression and Involvement in Disease.Journal of molecular biology · 2025Review
- Thiolutin has complex effects in vivo but is a direct inhibitor of RNA polymerase II in vitro.Nucleic acids research · 2024Article
- Identification of host proteins interacting with the E protein of porcine epidemic diarrhea virus.Frontiers in microbiology · 2024Article
- Evolutionary conservation of the fidelity of transcription.Nature communications · 2023Article
- Article
- A remodeled RNA polymerase II complex catalyzing viroid RNA-templated transcription.PLoS pathogens · 2022Article
- Interpretation of convolutional neural networks reveals crucial sequence features involving in transcription during fiber development.BMC bioinformatics · 2022Article
- Development of a Genetically Stable Live Attenuated Influenza Vaccine Strain Using an Engineered High-Fidelity Viral Polymerase.Journal of virology · 2021Article
- The RNA polymerase II subunit RPB-9 recruits the integrator complex to terminate Caenorhabditis elegans piRNA transcription.The EMBO journal · 2021Article
- Nucleotide Loading Modes of Human RNA Polymerase II as Deciphered by Molecular Simulations.Biomolecules · 2020Article
- High Transcriptional Error Rates Vary as a Function of Gene Expression Level.Genome biology and evolution · 2020Article
- The Mechanisms of Substrate Selection, Catalysis, and Translocation by the Elongating RNA Polymerase.Journal of molecular biology · 2019Review
- Transcription fidelity: New paradigms in epigenetic inheritance, genome instability and disease.DNA repair · 2019Review
- A Novel Assay for RNA Polymerase I Transcription Elongation Sheds Light on the Evolutionary Divergence of Eukaryotic RNA Polymerases.Biochemistry · 2019Article
- Functional assays for transcription mechanisms in high-throughput.Methods (San Diego, Calif.) · 2019Review
- Genome-wide Surveillance of Transcription Errors in Eukaryotic Organisms.Journal of visualized experiments : JoVE · 2018Article
- Structural basis of transcriptional stalling and bypass of abasic DNA lesion by RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Rpb9 is a small non-essential subunit of yeast RNA polymerase II located on the surface on the enzyme. Deletion of the RPB9 gene shows synthetic lethality with the low fidelity rpb1-E1103G mutation localized in the trigger loop, a mobile element of the catalytic Rpb1 subunit, which has been shown to control transcription fidelity. Similar to the rpb1-E1103G mutation, the RPB9 deletion substantially enhances NTP misincorporation and increases the rate of mismatch extension with the next cognate NTP in vitro. Using pre-steady state kinetic analysis, we show that RPB9 deletion promotes sequestration of NTPs in the polymerase active center just prior to the phosphodiester bond formation. We propose a model in which the Rpb9 subunit controls transcription fidelity by delaying the closure of the trigger loop on the incoming NTP via interaction between the C-terminal domain of Rpb9 and the trigger loop. Our findings reveal a mechanism for regulation of transcription fidelity by protein factors located at a large distance from the active center of RNA polymerase II.
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