Genetic and biochemical evidence shows that the basal transcription machinery of muscle cells invariably relies on TBP/TFIID because TBP2 is not expressed in muscle cells, and thus resolves a longstanding issue raised by previous conflicting data.

Proteasome-mediated degradation of the TATA-box binding protein (TBP) during terminal differentiation is regulated by the E3 ligase Huwe1 and the deubiquitinase USP10.

Integrative structural biology reveals a novel complex comprising the TATA-box-binding protein, TBP, and two subunits, TAF11 and TAF13, of General Transcription Factor TFIID, suggesting a new regulatory state in TFIID function in RNA polymerase II transcription initiation.

CBP/EP300 bromodomain inhibitors have a therapeutic application in oncology via targeting the IRF4 transcriptional program, a clinically validated network critical for multiple myeloma cell viability.

The general transcriptional machinery promotes the efficient reactivation of global transcription following mitosis, and thereby enables maintenance of transcriptional memory through the cell cycle.

Locally activatable bioluminescence (LABL) is a genetically encoded reporter that allows real time, in vivo measurement of distinct clocks in different cells and tissues in Drosophila.

A structural analysis of the transcription regulator Mot1 in complex with promoter DNA and the proteins TBP and NC2 provides a first structural framework for how a Swi2/Snf2 type remodeler interacts with a histone fold protein:DNA complex.

TATA-box binding protein is not required for RNA Polymerase II transcription in mouse embryonic stem cells.

CBP/p300 acetylation of histone H3 at promoters and enhancers stimulates transcriptional elongation through recruitment of the super-elongation complex and BRD4.

Loss of the RNA-binding protein TDP-43 impairs the survival of oligodendrocyte progenitors and reactivates growth of mature oligodendrocytes, resulting in inappropriate wrapping of neuronal somata and blood vessels.