Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

6YJ6

Structure of the TFIIIC subcomplex tauA

Summary for 6YJ6
Entry DOI10.2210/pdb6yj6/pdb
EMDB information10817
DescriptorTranscription 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 Keywordstfiiic, taua, transcription initiation, pol iii, tfiiib, transcription factor, transcription
Biological sourceSaccharomyces cerevisiae (Baker's yeast)
More
Total number of polymer chains3
Total formula weight247309.53
Authors
Vorlaender, M.K.,Muller, C.W. (deposition date: 2020-04-02, release date: 2020-09-16, Last modification date: 2024-05-22)
Primary citationVorlander, 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: 32999288
DOI: 10.1038/s41467-020-18707-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.1 Å)
Structure validation

238268

數據於2025-07-02公開中

PDB statisticsPDBj update infoContact PDBjnumon