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

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.

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

An inorganic tin oxochloride cluster specifically binds to an intrinsically disordered, histidine-rich, low complexity protein region and arrests de novo transcription initiation without affecting reinitiation.

The structure of the entire Mot1 Swi2/Snf2 protein uncovers an unexpected auto-inhibited resting state activated by substrate binding, and suggests a DNA pulling mechanism of TBP displacement.

Amino acid limitation triggers preferential uncharging of glutamine-specific tRNAs and depletes polyglutamine tract-containing proteins from mammalian cells, revealing a potential role for polyglutamine tracts as sensors of glutamine sufficiency.

The transcription machinery used to regulate gene expression and self-renewal in human embryonic stem cells is different from that found in other cells.

During epigenetic transcriptional memory in budding yeast, histone H3 lysine 4 dimethylation - dependent on Nup1000 and independent of RNA polymerase II - regulates binding of a critical transcription factor and, once established, is mitotically heritable for at least four cell divisions.

The transcription coactivators SAGA and TFIID have redundant function at a subset of yeast genes while SAGA also contributes to transcription of all genes through regulation of chromatin modifications.

Natural genetic variation reveals how DNA sequence impacts core transcriptional processes of initiation, pause, and termination.