ArticleBiochemistry2017
Multisubunit RNA Polymerase Cleavage Factors Modulate the Kinetics and Energetics of Nucleotide Incorporation: An RNA Polymerase I Case Study.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 27 citations in OpenAlex.
- TFIIS enhancement of Pol II cleavage is under kinetic control.Nucleic acids research · 2026Article
- Cryo-EM uncovers a sequential mechanism for RNA polymerase I pausing and stalling at abasic DNA lesions.Nature communications · 2025Article
- NTPs compete in the active site of RNA polymerases I and II.Biophysical chemistry · 2024Article
- Global kinetic mechanism describing single nucleotide incorporation for RNA polymerase I reveals fast UMP incorporation.Biophysical chemistry · 2024Article
- Reversible Kinetics in Multi-nucleotide Addition Catalyzed by S. cerevisiae RNA polymerase II Reveal Slow Pyrophosphate Release.Journal of molecular biology · 2024Article
- The A12.2 Subunit Plays an Integral Role in Pyrophosphate Release of RNA Polymerase I.Journal of molecular biology · 2023Article
- Transient-State Kinetic Analysis of the RNA Polymerase II Nucleotide Incorporation Mechanism.Biochemistry · 2023Article
- Article
- RNA polymerase I (Pol I) lobe-binding subunit Rpa12.2 promotes RNA cleavage and proofreading.The Journal of biological chemistry · 2022Article
- Multi-start Evolutionary Nonlinear OpTimizeR (MENOTR): A hybrid parameter optimization toolbox.Biophysical chemistry · 2021Article
- Article
- Transient-state kinetic analysis of multi-nucleotide addition catalyzed by RNA polymerase I.Biophysical journal · 2021Article
- The N-terminal domain of the A12.2 subunit stimulates RNA polymerase I transcription elongation.Biophysical journal · 2021Article
- Downstream sequence-dependent RNA cleavage and pausing by RNA polymerase I.The Journal of biological chemistry · 2020Article
- Coordinated Control of rRNA Processing by RNA Polymerase I.Trends in genetics : TIG · 2019Review
- Genetic analyses led to the discovery of a super-active mutant of the RNA polymerase I.PLoS genetics · 2019Article
- A Novel Assay for RNA Polymerase I Transcription Elongation Sheds Light on the Evolutionary Divergence of Eukaryotic RNA Polymerases.Biochemistry · 2019Article
- RNA polymerase III subunits C37/53 modulate rU:dA hybrid 3' end dynamics during transcription termination.Nucleic acids research · 2019Article
- The A12.2 Subunit Is an Intrinsic Destabilizer of the RNA Polymerase I Elongation Complex.Biophysical journal · 2018Article
- Defining the divergent enzymatic properties of RNA polymerases I and II.The Journal of biological chemistryArticle
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
All cellular RNA polymerases are influenced by protein factors that stimulate RNA polymerase-catalyzed cleavage of the nascent RNA. Despite divergence in amino acid sequence, these so-called "cleavage factors" appear to share a common mechanism of action. Cleavage factors associate with the polymerase through a conserved structural element of the polymerase known as the secondary channel or pore. This mode of association enables the cleavage factor to reach through the secondary channel into the polymerase active site to reorient the active site divalent metal ions. This reorientation converts the polymerase active site into a nuclease active site. Interestingly, eukaryotic RNA polymerases I and III (Pols I and III, respectively) have incorporated their cleavage factors as bona fide subunits known as A12.2 and C11, respectively. Although it is clear that A12.2 and C11 dramatically stimulate the polymerase's cleavage activity, it is not known if or how these subunits affect the polymerization mechanism. In this work we have used transient-state kinetic techniques to characterize a Pol I isoform lacking A12.2. Our data clearly demonstrate that the A12.2 subunit profoundly affects the kinetics and energetics of the elementary steps of Pol I-catalyzed nucleotide incorporation. Given the high degree of conservation between polymerase-cleavage factor interactions, these data indicate that cleavage factor-modulated nucleotide incorporation mechanisms may be common to all cellular RNA polymerases.
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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.