4wv4

Publication Abstract from PubMed

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.

Cytoplasmic TAF2-TAF8-TAF10 complex provides evidence for nuclear holo-TFIID assembly from preformed submodules.,Trowitzsch S, Viola C, Scheer E, Conic S, Chavant V, Fournier M, Papai G, Ebong IO, Schaffitzel C, Zou J, Haffke M, Rappsilber J, Robinson CV, Schultz P, Tora L, Berger I Nat Commun. 2015 Jan 14;6:6011. doi: 10.1038/ncomms7011. PMID:25586196^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.