6F3T

Crystal structure of the human TAF5-TAF6-TAF9 complex

Summary for 6F3T

• Entry DOI: 10.2210/pdb6f3t/pdb
• Descriptor: Transcription initiation factor TFIID subunit 5, Transcription initiation factor TFIID subunit 6, Transcription initiation factor TFIID subunit 9, ... (5 entities in total)
• Functional Keywords: transcription, complex, tfiid, taf, tbd-associated factor
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 12
• Total formula weight: 372905.60

Authors

Haffke, M.,Berger, I. (deposition date: 2017-11-28, release date: 2018-12-05, Last modification date: 2024-10-23)

Primary citation

Antonova, S.V.,Haffke, M.,Corradini, E.,Mikuciunas, M.,Low, T.Y.,Signor, L.,van Es, R.M.,Gupta, K.,Scheer, E.,Vos, H.R.,Tora, L.,Heck, A.J.R.,Timmers, H.T.M.,Berger, I.
Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly.
Nat. Struct. Mol. Biol., 25:1119-1127, 2018

PubMed Abstract: TFIID is a cornerstone of eukaryotic gene regulation. Distinct TFIID complexes with unique subunit compositions exist and several TFIID subunits are shared with other complexes, thereby conveying precise cellular control of subunit allocation and functional assembly of this essential transcription factor. However, the molecular mechanisms that underlie the regulation of TFIID remain poorly understood. Here we use quantitative proteomics to examine TFIID submodules and assembly mechanisms in human cells. Structural and mutational analysis of the cytoplasmic TAF5-TAF6-TAF9 submodule identified novel interactions that are crucial for TFIID integrity and for allocation of TAF9 to TFIID or the Spt-Ada-Gcn5 acetyltransferase (SAGA) co-activator complex. We discover a key checkpoint function for the chaperonin CCT, which specifically associates with nascent TAF5 for subsequent handover to TAF6-TAF9 and ultimate holo-TFIID formation. Our findings illustrate at the molecular level how multisubunit complexes are generated within the cell via mechanisms that involve checkpoint decisions facilitated by a chaperone.

PubMed: 30510221
DOI: 10.1038/s41594-018-0156-z

Experimental method

X-RAY DIFFRACTION (2.5 Å)