The conformational state of the nucleosome entry-exit site modulates TATA box-specific TBP binding.

ABSTRACT: The TATA binding protein (TBP) is a critical transcription factor used for nucleating assembly of the RNA polymerase II machinery. TBP binds TATA box elements with high affinity and kinetic stability and in vivo is correlated with high levels of transcription activation. However, since most promoters use less stable TATA-less or TATA-like elements, while also competing with nucleosome occupancy, further mechanistic insight into TBP's DNA binding properties and ability to access chromatin is needed. Using bulk and single-molecule FRET, we find that TBP binds a minimal consensus TATA box as a two-state equilibrium process, showing no evidence for intermediate states. However, upon addition of flanking DNA sequence, we observe non-specific cooperative binding to multiple DNA sites that compet

SUBMITTER: Hieb AR 

PROVIDER: S-EPMC4081063 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature