4WV4

Heterodimer of TAF8/TAF10

Summary for 4WV4

• Entry DOI: 10.2210/pdb4wv4/pdb
• Descriptor: Transcription initiation factor TFIID subunit 10, Transcription initiation factor TFIID subunit 8, GLYCEROL, ... (5 entities in total)
• Functional Keywords: transcription, tbp-associated factor, heterodimer, histone fold domain
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q12962 Q7Z7C8
• Total number of polymer chains: 2
• Total formula weight: 22170.57

Authors

Trowitzsch, S. (deposition date: 2014-11-04, release date: 2015-01-28, Last modification date: 2024-05-08)

Primary citation

Trowitzsch, S.,Viola, C.,Scheer, E.,Conic, S.,Chavant, V.,Fournier, M.,Papai, G.,Ebong, I.O.,Schaffitzel, C.,Zou, J.,Haffke, M.,Rappsilber, J.,Robinson, C.V.,Schultz, P.,Tora, L.,Berger, I.
Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.
Nat Commun, 6:6011-6011, 2015

PubMed Abstract: General transcription factor TFIID is a cornerstone of RNA polymerase II transcription initiation in eukaryotic cells. How human TFIID-a megadalton-sized multiprotein complex composed of the TATA-binding protein (TBP) and 13 TBP-associated factors (TAFs)-assembles into a functional transcription factor is poorly understood. Here we describe a heterotrimeric TFIID subcomplex consisting of the TAF2, TAF8 and TAF10 proteins, which assembles in the cytoplasm. Using native mass spectrometry, we define the interactions between the TAFs and uncover a central role for TAF8 in nucleating the complex. X-ray crystallography reveals a non-canonical arrangement of the TAF8-TAF10 histone fold domains. TAF2 binds to multiple motifs within the TAF8 C-terminal region, and these interactions dictate TAF2 incorporation into a core-TFIID complex that exists in the nucleus. Our results provide evidence for a stepwise assembly pathway of nuclear holo-TFIID, regulated by nuclear import of preformed cytoplasmic submodules.

PubMed: 25586196
DOI: 10.1038/ncomms7011

Experimental method

X-RAY DIFFRACTION (1.909 Å)