English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Conserved RNA polymerase II initiation complex structure.

MPS-Authors
/persons/resource/persons195451

Hantsche,  M.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons127020

Cramer,  P.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)

2426488.pdf
(Publisher version), 2MB

Supplementary Material (public)
There is no public supplementary material available
Citation

Hantsche, M., & Cramer, P. (2017). Conserved RNA polymerase II initiation complex structure. Current Opinion in Structural Biology, 47, 17-22. doi:10.1016/j.sbi.2017.03.013.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-1D96-C
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.