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Chaperonin CCT checkpoint function in basal transcription factor TFIID assembly

A combination of proteomics and structural analyses reveals the assembly mechanism of transcription factor TFIID in human cells and identifies the chaperonin CCT as a checkpoint in the process.

Simona V. Antonova
Matthias Haffke
Imre Berger
Research03 Dec 2018
Nature Structural & Molecular Biology

Volume: 25, P: 1119-1127
Structural basis of species-selective antagonist binding to the succinate receptor

High-resolution crystal structures of the rat succinate receptor SUCNR1 in an inactive confirmation, and the humanized rat SUCNR1 bound to an antagonist, provide insights into the structure of these receptors and the species selectivity of antagonist binding.

Matthias Haffke
Dominique Fehlmann
Veli-Pekka Jaakola
Research23 Oct 2019
Nature

Volume: 574, P: 581-585
Cytoplasmic TAF2–TAF8–TAF10 complex provides evidence for nuclear holo–TFIID assembly from preformed submodules

TFIID is an essential transcription factor complex that controls the expression of most protein-coding genes in eukaryotes. Here the authors identify and characterize a complex containing TAF2, TAF8 and TAF10, which assembles in the cytoplasm before integration into the nuclear holo–TFIID complex.

Simon Trowitzsch
Cristina Viola
Imre Berger
ResearchOpen Access14 Jan 2015
Nature Communications

Volume: 6, P: 1-14

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