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-Structure paper
Title | Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation. |
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Journal, issue, pages | Mol Cell, Vol. 83, Issue 15, Page 2641-22652.e7, Year 2023 |
Publish date | Aug 3, 2023 |
Authors | Anna Talyzina / Yan Han / Chiranjib Banerjee / Susan Fishbain / Alexis Reyes / Reza Vafabakhsh / Yuan He / |
PubMed 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 ...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. |
External links | Mol Cell / PubMed:37402369 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.8 - 7.14 Å |
Structure data | EMDB-29071, PDB-8ffz: EMDB-29356: Focused refinement on the Brf1-TBP-DNA within TFIIIA-TFIIIC-Brf1-TBP complex bound to 5S rRNA gene EMDB-29358: TFIIIA-TFIIIC complex bound to 5S rRNA gene |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | TRANSCRIPTION/DNA / transcription factor / TRANSCRIPTION / TRANSCRIPTION-DNA complex |