ArticleThe Journal of biological chemistry2011
Evolution of two modes of intrinsic RNA polymerase transcript cleavage.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 78 citations in OpenAlex.
- TFIIS enhancement of Pol II cleavage is under kinetic control.Nucleic acids research · 2026Article
- Transcription fidelity and control of alternative splicing contribute to heat stress survival in Arabidopsis.The Plant cell · 2025Article
- The Nucleolus: A Central Hub for Ribosome Biogenesis and Cellular Regulatory Signals.International journal of molecular sciences · 2025Review
- TFIIS is required for reproductive development and thermal adaptation in barley.Plant cell reports · 2024Article
- Reversible Kinetics in Multi-nucleotide Addition Catalyzed by S. cerevisiae RNA polymerase II Reveal Slow Pyrophosphate Release.Journal of molecular biology · 2024Article
- DNA-dependent RNA polymerases in plants.The Plant cell · 2023Article
- The A12.2 Subunit Plays an Integral Role in Pyrophosphate Release of RNA Polymerase I.Journal of molecular biology · 2023Article
- Structural basis of Ty1 integrase tethering to RNA polymerase III for targeted retrotransposon integration.Nature communications · 2023Article
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- RNA polymerase I (Pol I) lobe-binding subunit Rpa12.2 promotes RNA cleavage and proofreading.The Journal of biological chemistry · 2022Article
- Evolution of the RNA Cleavage Subunit C11/RPC10, and Recycling by RNA Polymerase III.Journal of cellular immunology · 2022Article
- Cryo-EM structures of human RNA polymerase I.Nature structural & molecular biology · 2021Article
- Conserved Trigger Loop Histidine of RNA Polymerase II Functions as a Positional Catalyst Primarily through Steric Effects.Biochemistry · 2021Article
- β-CASP proteins removing RNA polymerase from DNA: when a torpedo is needed to shoot a sitting duck.Nucleic acids research · 2021Review
- Collaboration through chromatin: motors of transcription and chromatin structure.Journal of molecular biology · 2021Review
- The N-terminal domain of the A12.2 subunit stimulates RNA polymerase I transcription elongation.Biophysical journal · 2021Article
- Structural insights into transcriptional regulation of human RNA polymerase III.Nature structural & molecular biology · 2021Article
- Specific Features of RNA Polymerases I and III: Structure and Assembly.Frontiers in molecular biosciences · 2021Review
- Critical Role of Transcript Cleavage in Arabidopsis RNA Polymerase II Transcriptional Elongation.The Plant cell · 2020Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During gene transcription, the RNA polymerase (Pol) active center can catalyze RNA cleavage. This intrinsic cleavage activity is strong for Pol I and Pol III but very weak for Pol II. The reason for this difference is unclear because the active centers of the polymerases are virtually identical. Here we show that Pol II gains strong cleavage activity when the C-terminal zinc ribbon domain (C-ribbon) of subunit Rpb9 is replaced by its counterpart from the Pol III subunit C11. X-ray analysis shows that the C-ribbon has detached from its site on the Pol II surface and is mobile. Mutagenesis indicates that the C-ribbon transiently inserts into the Pol II pore to complement the active center. This mechanism is also used by transcription factor IIS, a factor that can bind Pol II and induce strong RNA cleavage. Together with published data, our results indicate that Pol I and Pol III contain catalytic C-ribbons that complement the active center, whereas Pol II contains a non-catalytic C-ribbon that is immobilized on the enzyme surface. Evolution of the Pol II system may have rendered mRNA transcript cleavage controllable by the dissociable factor transcription factor IIS to enable promoter-proximal gene regulation and elaborate 3'-processing and transcription termination.
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