8FFZ
TFIIIA-TFIIIC-Brf1-TBP complex bound to 5S rRNA gene
Summary for 8FFZ
| Entry DOI | 10.2210/pdb8ffz/pdb |
| EMDB information | 29071 |
| Descriptor | Transcription factor IIIA, DNA (151-MER), ZINC ION, ... (11 entities in total) |
| Functional Keywords | transcription factor, transcription, transcription-dna complex, transcription/dna |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 10 |
| Total formula weight | 758888.90 |
| Authors | Talyzina, A.,He, Y. (deposition date: 2022-12-11, release date: 2023-06-21, Last modification date: 2023-08-16) |
| Primary citation | Talyzina, A.,Han, Y.,Banerjee, C.,Fishbain, S.,Reyes, A.,Vafabakhsh, R.,He, Y. Structural basis of TFIIIC-dependent RNA polymerase III transcription initiation. Mol.Cell, 83:2641-, 2023 Cited by 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 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. PubMed: 37402369DOI: 10.1016/j.molcel.2023.06.015 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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