ArticleBiophysical journal2018
The A12.2 Subunit Is an Intrinsic Destabilizer of the RNA Polymerase I Elongation Complex.
Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 31 citations in OpenAlex.
- TFIIS enhancement of Pol II cleavage is under kinetic control.Nucleic acids research · 2026Article
- Kinetic characterization of RNA synthesis catalyzed by the model hyperthermophilic archaeonmSphere · 2025Article
- 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
- Regulation of RNA Polymerase I Stability and Function.Cancers · 2022Review
- Uncovering the mechanisms of transcription elongation by eukaryotic RNA polymerases I, II, and III.iScience · 2022Article
- Article
- RNA polymerase I (Pol I) lobe-binding subunit Rpa12.2 promotes RNA cleavage and proofreading.The Journal of biological chemistry · 2022Article
- Specialization of RNA Polymerase I in Comparison to Other Nuclear RNA Polymerases of Saccharomyces cerevisiae.Methods in molecular biology (Clifton, N.J.) · 2022Review
- 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
- Coupling Between Production of Ribosomal RNA and Maturation: Just at the Beginning.Frontiers in molecular biosciences · 2021Review
- Downstream sequence-dependent RNA cleavage and pausing by RNA polymerase I.The Journal of biological chemistry · 2020Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Despite sharing a highly conserved core architecture with their prokaryotic counterparts, eukaryotic multisubunit RNA polymerases (Pols) have undergone structural divergence and biological specialization. Interesting examples of structural divergence are the A12.2 and C11 subunits of Pols I and III, respectively. Whereas all known cellular Pols possess cognate protein factors that stimulate cleavage of the nascent RNA, Pols I and III have incorporated their cleavage factors as bona fide subunits. Although it is not yet clear why these polymerases have incorporated their cleavage factors as subunits, a picture is emerging that identifies roles for these subunits beyond providing nucleolytic activity. Specifically, it appears that both A12.2 and C11 are required for efficient termination of transcription by Pols I and III. Given that termination involves destabilization of the elongation complex (EC), we tested whether A12.2 influences stability of the Pol I EC. Using, to our knowledge, a novel assay to measure EC dissociation kinetics, we have determined that A12.2 is an intrinsic destabilizer of the Pol I EC. In addition, the salt concentration dependence of Pol I EC dissociation kinetics suggests that A12.2 alters electrostatic interactions within the EC. Importantly, these data present a mechanistic basis for the requirement of A12.2 in Pol I termination. Combined with recent work demonstrating the direct involvement of A12.2 in Pol I nucleotide incorporation, this study further supports the concept that A12.2 cannot be viewed solely as a cleavage factor.
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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.