ArticleGenes & development1998
The RNA cleavage activity of RNA polymerase III is mediated by an essential TFIIS-like subunit and is important for transcription termination.
Article in Genes & development, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed, 169 citations in OpenAlex.
- New biomarkers for the detection of fetal death derived from large-scale proteomic analysis of maternal plasma.American journal of obstetrics and gynecology · 2026Article
- Terminator-dependent facilitated recycling of RNA polymerase III provides gene-specific transcriptional activation in vivo.Science advances · 2026Article
- Human RNA polymerase III termination favors decomposition over facilitated recycling.Nature communications · 2026Article
- Article
- Differential impact of divalent metals on native elongating transcript sequencing (NET-seq) protocols for RNA polymerases I and II.PloS one · 2025Article
- Improved prime editing allows for routine predictable gene editing in Physcomitrium patens.Journal of experimental botany · 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
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- A structural perspective of human RNA polymerase III.RNA biology · 2022Article
- The BORDER family of negative transcription elongation factors regulates flowering time in Arabidopsis.Current biology : CB · 2021Article
- The nuclear and cytoplasmic activities of RNA polymerase III, and an evolving transcriptome for surveillance.Nucleic acids research · 2021Article
- Structural insights into RNA polymerase III-mediated transcription termination through trapping poly-deoxythymidine.Nature communications · 2021Article
- Mechanism of RNA polymerase III termination-associated reinitiation-recycling conferred by the essential function of the N terminal-and-linker domain of the C11 subunit.Nature communications · 2021Article
- Structure of human RNA polymerase III elongation complex.Cell research · 2021Article
- RNA Sequence and Structure Determinants of Pol III Transcriptional Termination in Human Cells.Journal of molecular biology · 2021Article
- Activation and repression at the heart of human RNA polymerase III.Nature structural & molecular biology · 2021Article
- Structural insights into transcriptional regulation of human RNA polymerase III.Nature structural & molecular biology · 2021Article
- Cryo-EM structures of human RNA polymerase III in its unbound and transcribing states.Nature structural & molecular biology · 2021Article
- Eukaryotic RNA Polymerases: The Many Ways to Transcribe a Gene.Frontiers in molecular biosciences · 2021Review
30 more citing papers are in PubMed but not listed here.
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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
Budding yeast RNA polymerase III (Pol III) contains a small, essential subunit, named C11, that is conserved in humans and shows a strong homology to TFIIS. A mutant Pol III, heterocomplemented with Schizosaccharomyces pombe C11, was affected in transcription termination in vivo. A purified form of the enzyme (Pol III Delta), deprived of C11 subunit, initiated properly but ignored pause sites and was defective in termination. Remarkably, Pol III Delta lacked the intrinsic RNA cleavage activity of complete Pol III. In vitro reconstitution experiments demonstrated that Pol III RNA cleavage activity is mediated by C11. Mutagenesis in C11 of two conserved residues, which are critical for the TFIIS-dependent cleavage activity of Pol II, is lethal. Immunoelectron microscopy data suggested that C11 is localized on the mobile thumb-like stalk of the polymerase. We propose that C11 allows the enzyme to switch between an RNA elongation and RNA cleavage mode and that the essential role of the Pol III RNA cleavage activity is to remove the kinetic barriers to the termination process. The integration of TFIIS function into a specific Pol III subunit may stem from the opposite requirements of Pol III and Pol II in terms of transcript length and termination efficiency.
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