Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules - Archive ouverte HAL Access content directly
Journal Articles Nature Communications Year : 2015

Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

Juan Zou
  • Function : Author
Carol Robinson

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.
Fichier principal
Vignette du fichier
ncomms7011.pdf (2.06 Mo) Télécharger le fichier
Origin Publication funded by an institution

Dates and versions

hal-03457219 , version 1 (04-01-2024)

Identifiers

Cite

Simon Trowitzsch, Cristina Viola, Elisabeth Scheer, Sascha Conic, Virginie Chavant, et al.. Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules. Nature Communications, 2015, 6 (1), ⟨10.1038/ncomms7011⟩. ⟨hal-03457219⟩
15 View
7 Download

Altmetric

Share

Gmail Mastodon Facebook X LinkedIn More