Conserved RNA polymerase II initiation complex structure. (December 2017)

• Record Type: Journal Article
• Authors: Hantsche, Merle; Cramer, Patrick
• Is Part Of: Current opinion in structural biology. Volume 47(2017)
• Page Start: 17
• Page End: 22
• Publication Date: 2017-12
• Subjects: Molecular biology -- Periodicals; 570
• DOI: 10.1016/j.sbi.2017.03.013
• Languages: English
• ISSNs: 0959-440X

Abstract

Highlights: Recent high-resolution cryo-EM structures reveal that human and yeast core initiation complexes are highly conserved. Atomic models show an intricate network of interactions between Pol II, transcription factors and DNA. A topological model of the complete Pol II initiation assembly including TFIIH, TFIID and Mediator can be derived. Abstract : Recent cryo-electron microscopic studies have arrived at atomic models of the core transcription initiation complex comprising RNA polymerase (Pol) II and the basal transcription factors TBP, TFIIA, TFIIB, TFIIE, and TFIIF. A detailed comparison of two independently derived yeast and human core initiation complex structures reveals that they are virtually identical, demonstrating the conservation of the basic transcription machinery amongst eukaryotes. The additional factors TFIID, TFIIH, and Mediator have been located on the periphery of the core initiation complex, providing the topology of the entire initiation assembly, which comprises approximately 70 polypeptides with a molecular weight of ∼4 Megadalton.