6YJ6
Structure of the TFIIIC subcomplex tauA
Summary for 6YJ6
Entry DOI | 10.2210/pdb6yj6/pdb |
EMDB information | 10817 |
Descriptor | Transcription factor tau 131 kDa subunit, Transcription factor tau 95 kDa subunit,Transcription factor tau 95 kDa subunit, Transcription factor tau 55 kDa subunit (3 entities in total) |
Functional Keywords | tfiiic, taua, transcription initiation, pol iii, tfiiib, transcription factor, transcription |
Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
Total number of polymer chains | 3 |
Total formula weight | 247309.53 |
Authors | Vorlaender, M.K.,Muller, C.W. (deposition date: 2020-04-02, release date: 2020-09-16, Last modification date: 2024-05-22) |
Primary citation | Vorlander, M.K.,Jungblut, A.,Karius, K.,Baudin, F.,Grotsch, H.,Kosinski, J.,Muller, C.W. Structure of the TFIIIC subcomplex tau A provides insights into RNA polymerase III pre-initiation complex formation. Nat Commun, 11:4905-4905, 2020 Cited by PubMed Abstract: Transcription factor (TF) IIIC is a conserved eukaryotic six-subunit protein complex with dual function. It serves as a general TF for most RNA polymerase (Pol) III genes by recruiting TFIIIB, but it is also involved in chromatin organization and regulation of Pol II genes through interaction with CTCF and condensin II. Here, we report the structure of the S. cerevisiae TFIIIC subcomplex τA, which contains the most conserved subunits of TFIIIC and is responsible for recruitment of TFIIIB and transcription start site (TSS) selection at Pol III genes. We show that τA binding to its promoter is auto-inhibited by a disordered acidic tail of subunit τ95. We further provide a negative-stain reconstruction of τA bound to the TFIIIB subunits Brf1 and TBP. This shows that a ruler element in τA achieves positioning of TFIIIB upstream of the TSS, and suggests remodeling of the complex during assembly of TFIIIB by TFIIIC. PubMed: 32999288DOI: 10.1038/s41467-020-18707-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.1 Å) |
Structure validation
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