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Cited by 15Genomics and Chromatin DynamicsNuclear Structure and FunctionRNA and protein synthesis mechanisms

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Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation

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Talyzina, Anna, Han, Yan, Banerjee, Chiranjib, Fishbain, Susan, Reyes, Alexis, Vafabakhsh, Reza, He, Yuan·2023·Molecular Cell
DOI 10.1016/j.molcel.2023.06.015PMC PMC10528418

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Abstract

RNA polymerase III (Pol III) is responsible for transcribing 5S ribosomal RNA (5S rRNA), tRNAs, and other short non-coding RNAs. Its recruitment to the 5S rRNA promoter requires transcription factors TFIIIA, TFIIIC, and TFIIIB. Here, we use cryoelectron microscopy (cryo-EM) to visualize the S. cerevisiae complex of TFIIIA and TFIIIC bound to the promoter. Gene-specific factor TFIIIA interacts with DNA and acts as an adaptor for TFIIIC-promoter interactions. We also visualize DNA binding of TFIIIB subunits, Brf1 and TBP (TATA-box binding protein), which results in the full-length 5S rRNA gene wrapping around the complex. Our smFRET study reveals that the DNA within the complex undergoes both sharp bending and partial dissociation on a slow timescale, consistent with the model predicted from our cryo-EM results. Our findings provide new insights into the transcription initiation complex assembly on the 5S rRNA promoter and allow us to directly compare Pol III and Pol II transcription adaptations.

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Metadata

Authors
Talyzina, A., Han, Y., Banerjee, C., Fishbain, S., Reyes, A., Vafabakhsh, R., & He, Y.
Affiliations
Northwestern University (US)
Corresponding author
He, Yuan
ORCID
Venue
Molecular Cell
Publisher
Elsevier BV
Published
2023-08
Volume
83
Issue
15
Pages
2641-2652.e7
ISSN
1097-2765 (ISSN-L)
DOI
10.1016/j.molcel.2023.06.015
PMC
PMC10528418
OpenAlex
W4382988705
Cited by
15
References
1
Citations by year
2026: 5 · 2025: 3 · 2024: 6 · 2023: 1
FWCI
1.34
Type
journal article
Language
en
Open access
Licence
Locations
  • Molecular Cell (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • OSTI OAI (U.S. Department of Energy Office of Scientific and Technical Information) (submittedVersion)
  • PubMed Central (submittedVersion, cc-by-nc-nd)
Funders
  • National Institutes of Health (U24GM129547)
  • National Cancer Institute (P01CA092584)
  • American Cancer Society (IRG-15-173-21)
  • Biological and Environmental Research (CCSG P30 CA060553)
  • National Institute of General Medical Sciences (R01GM140272, R01GM135651, R01GM144559)
  • Northwestern University
  • Oregon Health and Science University
  • Office of Science
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords
RNA polymerase III, transcription initiation, TFIIIC, TFIIIA, TFIIIB, promoter binding, Brf1, TATA-binding protein, DNA bending, DNA dissociation, Saccharomyces cerevisiae, single-molecule FRET

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