Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 118, Issue 30, Pages -Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.2108859118
Keywords
gene transcription RNA polymerase II nucleosome chromatin structural biology
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Funding
- International Max Planck Reseach School for Genome Science
- Deutsche Forschungsgemeinschaft [SFB860, SPP2191, EXC 2067/1-390729940]
- European Research Council Advanced Investigator Grant CHROMATRANS [882357]
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TBP, a highly conserved protein, plays a central role in assembling the transcription preinitiation complex (PIC). TBP can bind to diverse nucleosome positions and its binding is stabilized by TFIIA. However, TBP-nucleosome complexes are incompatible with PIC assembly and must be removed before transcription initiation.
The TATA box-binding protein (TBP) is highly conserved throughout eukaryotes and plays a central role in the assembly of the transcription preinitiation complex (PIC) at gene promoters. TBP binds and bends DNA, and directs adjacent binding of the transcription factors TFIIA and TFIIB for PIC assembly. Here, we show that yeast TBP can bind to a nucleosome containing the Widom601 sequence and that TBP-nucleosome binding is stabilized by TFIIA. We determine three cryo-electron microscopy (cryo-EM) structures of TBP-nucleosome complexes, two of them containing also TFIIA. TBP can bind to superhelical location (SHL) -6, which contains a TATA-like sequence, but also to SHL +2, which is GC rich. Whereas binding to SHL -6 can occur in the absence of TFIIA, binding to SHL +2 is only observed in the presence of TFIIA and goes along with detachment of upstream terminal DNA from the histone octamer. TBP-nucleosome complexes are sterically incompatible with PIC assembly, explaining why a promoter nucleosome generally impairs transcription and must be moved before initiation can occur.
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