ArticleNucleic acids research2018
Function of TFIIIC, RNA polymerase III initiation factor, in activation and repression of tRNA gene transcription.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Modification of the Transcription Factor FOXL2 at Serines 101 and 107 Disables DNA Binding, Leads to Nucleolar Relocalization, and Rewires Granulosa-Cell Programs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Serine tRNAs compete to regulate the mRNA translation of serine-sensitive codons.Science advances · 2025Article
- Should I stay or should I go: TFIIIC as assembly factor and barrier in RNA polymerase III transcription.Biochemical Society transactions · 2025Review
- Rise and SINE: roles of transcription factors and retrotransposons in zygotic genome activation.Nature reviews. Molecular cell biology · 2025Article
- Evidence of RNA polymerase III recruitment and transcription at protein-coding gene promoters.Molecular cell · 2024Article
- The choreography of chromatin in RNA polymerase III regulation.Biochemical Society transactions · 2024Review
- tRNA Modifications and Dysregulation: Implications for Brain Diseases.Brain sciences · 2024Review
- Evidence of RNA polymerase III recruitment and transcription at protein-coding gene promoters.bioRxiv : the preprint server for biology · 2024Article
- Locus-specific proteome decoding reveals Fpt1 as a chromatin-associated negative regulator of RNA polymerase III assembly.Molecular cell · 2023Article
- Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation.Molecular cell · 2023Article
- Mutational and biophysical analyses reveal a TFIIIC binding region in the TFIIF-related Rpc53 subunit of RNA polymerase III.The Journal of biological chemistry · 2023Article
- Structural basis of TFIIIC-dependent RNA Polymerase III transcription initiation.bioRxiv : the preprint server for biology · 2023Article
- Structural insights into nuclear transcription by eukaryotic DNA-dependent RNA polymerases.Nature reviews. Molecular cell biology · 2022Review
- Pol3Base: a resource for decoding the interactome, expression, evolution, epitranscriptome and disease variations of Pol III-transcribed ncRNAs.Nucleic acids research · 2022Article
- Transcription recycling assays identify PAF1 as a driver for RNA Pol II recycling.Nature communications · 2021Article
- Alternate Roles of Sox Transcription Factors beyond Transcription Initiation.International journal of molecular sciences · 2021Review
- Specific Features of RNA Polymerases I and III: Structure and Assembly.Frontiers in molecular biosciences · 2021Review
- On the Track of the Missing tRNA Genes: A Source of Non-Canonical Functions?Frontiers in molecular biosciences · 2021Review
- Structure of the TFIIIC subcomplex τA provides insights into RNA polymerase III pre-initiation complex formation.Nature communications · 2020Article
- Inhibition of tRNA Gene Transcription by the Immunosuppressant Mycophenolic Acid.Molecular and cellular biology · 2019Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcription of transfer RNA genes by RNA polymerase III (Pol III) is controlled by general factors, TFIIIB and TFIIIC, and a negative regulator, Maf1. Here we report the interplay between TFIIIC and Maf1 in controlling Pol III activity upon the physiological switch of yeast from fermentation to respiration. TFIIIC directly competes with Pol III for chromatin occupancy as demonstrated by inversely correlated tDNA binding. The association of TFIIIC with tDNA was stronger under unfavorable respiratory conditions and in the presence of Maf1. Induction of tDNA transcription by glucose-activated protein kinase A (PKA) was correlated with the down-regulation of TFIIIC occupancy on tDNA. The conditions that activate the PKA signaling pathway promoted the binding of TFIIIB subunits, Brf1 and Bdp1, with tDNA, but decreased their interaction with TFIIIC. Association of Brf1 and Bdp1 with TFIIIC was much stronger under repressive conditions, potentially restricting TFIIIB recruitment to tDNA and preventing Pol III recruitment. Altogether, we propose a model in which, depending on growth conditions, TFIIIC promotes activation or repression of tDNA transcription.
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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.