4.8 Article

An integrated model for termination of RNA polymerase III transcription

Journal

SCIENCE ADVANCES
Volume 8, Issue 28, Pages -

Publisher

AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/sciadv.abm9875

Keywords

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Funding

  1. Centre National de la Recherche Scientifique
  2. Agence National pour la Recherche [ANR-16-CE12-0001-01]
  3. Agence National pour la Recherche grant [ANR-16-CE12-0022-01]
  4. Fondation pour la Recherche Medical funding
  5. China Scholarship Council PhD fellowship
  6. Fondation pour la Recherche Medical PhD fellowship [FDT202012010433]
  7. LabEx Who Am I? (Universite de Paris IdEx) postdoctoral fellowship [ANR-18-IDEX-0001]
  8. French Ministry of Education and Research PhD fellowship
  9. Fondation ARC pour la recherche sur le cancer PhD fellowship
  10. Boehringer Ingelheim Fonds PhD fellowship
  11. EMBL International PhD program
  12. EMBL funding
  13. Deutsche Forschungsgemeinschaft [PE 2079/2-2]
  14. LabEx Who Am I? postdoctoral fellowship [ANR-11-LABX-0071]
  15. Agence Nationale de la Recherche (ANR) [ANR-16-CE12-0022, ANR-16-CE12-0001] Funding Source: Agence Nationale de la Recherche (ANR)

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RNA polymerase III utilizes multiple mechanisms, including the recognition of T-tracts, the secondary structure of nascent RNAs, and the helicase Sen1, to ensure efficient transcription termination.
RNA polymerase III (RNAPIII) synthesizes essential and abundant noncoding RNAs such as transfer RNAs. Controlling RNAPIII span of activity by accurate and efficient termination is a challenging necessity to ensure robust gene expression and to prevent conflicts with other DNA-associated machineries. The mechanism of RNAPIII termination is believed to be simpler than that of other eukaryotic RNA polymerases, solely relying on the recognition of a T-tract in the nontemplate strand. Here, we combine high-resolution genome-wide analyses and in vitro transcription termination assays to revisit the mechanism of RNAPIII transcription termination in budding yeast. We show that T-tracts are necessary but not always sufficient for termination and that secondary structures of the nascent RNAs are important auxiliary cis-acting elements. Moreover, we show that the helicase Sen1 plays a key role in a fail-safe termination pathway. Our results provide a comprehensive model illustrating how multiple mechanisms cooperate to ensure efficient RNAPIII transcription termination.

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