Complete RNA polymerase II elongation complex structure and its interactions 
with NTP and TFIIS.

Kettenberger, H.; Armache, K. J.; Cramer, P.

doi:10.1016/j.molcel.2004.11.040

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS.

MPS-Authors

/persons/resource/persons127020

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

External Resource

http://www.sciencedirect.com/science/article/pii/S1097276504007300/pdfft?md5=c9add8ced8f0313a1ab3dc1e8034c975&pid=1-s2.0-S1097276504007300-main.pdf
(Publisher version)

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

1940653.pdf
(Publisher version), 928KB

Supplementary Material (public)

There is no public supplementary material available

Citation

Kettenberger, H., Armache, K. J., & Cramer, P. (2004). Complete RNA polymerase II elongation complex structure and its interactions with NTP and TFIIS. Molecular Cell, 16(6), 955-965. doi:10.1016/j.molcel.2004.11.040.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0015-84E1-D

Abstract

The crystal structure of the complete 12 subunit RNA polymerase (pol) II bound to a transcription bubble and product RNA reveals incoming template and non-template DNA, a seven base pair DNA/RNA hybrid, and three nucleotides each of separating DNA and RNA. The complex adopts the posttranslocation state and accommodates a cocrystallized nucleoside triphosphate (NTP) substrate. The NTP binds in the active site pore at a position to interact with a DNA template base. Residues surrounding the NTP are conserved in all cellular RNA polymerases, suggesting a universal mechanism of NTP selection and incorporation. DNA-DNA and DNA-RNA strand separation may be explained by pol II-induced duplex distortions. Four protein loops partition the active center cleft, contribute to embedding the hybrid, prevent strand reassociation, and create an RNA exit tunnel. Binding of the elongation factor TFIIS realigns RNA in the active center, possibly converting the elongation complex to an alternative state less prone to stalling.