Evidence and sources
Each number on the RNA polymerase II page goes back to an experiment or a calculation. Each card shows the result, how it was measured, and where it was published.
Measurements
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Big picture numbers
Structures
- 5C4XYeast Pol II elongation complex with a complete bubbleThe complete transcription bubble in one entry: both DNA strands and the RNA, on all twelve subunits. X-ray diffraction, 4 Å.
- 1I50Free yeast Pol II, clamp openThe clamp is open here, which lets straight DNA into the cleft. It is the start state for the clamp-closing morph. X-ray diffraction, 2.8 Å.
- 1I6HYeast Pol II elongation complex, clamp closedThe same ten subunits as the free enzyme, with nucleic acid bound and the clamp closed. It pairs with 1I50 for a morph. X-ray diffraction, 3.3 Å.
- 2E2HPol II elongation complex with GTP in the active siteShows the substrate in the addition site, the state that closes the trigger loop over the nucleotide. X-ray diffraction, 3.95 Å.
- 2VUMPol II elongation complex inhibited by alpha-amanitinThe drug traps the enzyme with a shifted bridge helix and a wedged trigger loop, which shows how translocation is blocked. X-ray diffraction, 3.4 Å.
- 1K83Yeast Pol II with alpha-amanitinThe first view of the amanitin site, next to the bridge helix. X-ray diffraction, 2.8 Å.
- 5FLMMammalian Pol II elongation complexThe mammalian enzyme in the act of transcribing, for a species comparison with yeast. Electron microscopy, 3.4 Å.
- 2O5IBacterial RNA polymerase elongation complexThe bacterial comparison: five subunit types instead of twelve, with the same two-metal active site. The DNA template is in the active site, ready to pair with substrate. X-ray diffraction, 2.5 Å.
- 2O5JBacterial elongation complex with substrate analogueSame crystal form as 2O5I with substrate bound, so the trigger-loop folding step can be morphed. X-ray diffraction, 3 Å.
- 2PPBBacterial elongation complex with streptolydiginShows an inactive pre-insertion substrate position, the state an antibiotic can freeze. X-ray diffraction, 3 Å.
- 6RH3E. coli RNA polymerase elongation complex with CTPAn E. coli elongation complex with clearly named template and non-template strands. Electron microscopy, 3.6 Å.
- 1MSWT7 RNA polymerase elongation complexThe single-subunit phage enzyme used for orthogonal expression. It shows how small a working polymerase can be. X-ray diffraction, 2.1 Å.
References
- 1Cramer et al., Science 2001
- 2Gnatt et al., Science 2001
- 3Bushnell and Kornberg, PNAS 2003
- 4Bushnell et al., PNAS 2002
- 5Brueckner and Cramer, Nature Structural and Molecular Biology 2008
- 6Wang et al., Cell 2006
- 7Vassylyev et al., Nature 2007, 448, 157-162
- 8Vassylyev et al., Nature 2007, 448, 163-168
- 9Sydow and Cramer, Current Opinion in Structural Biology 2009
- 10Sydow et al., Molecular Cell 2009
- 11Thomas et al., Cell 1998
- 12Cheung and Cramer, Nature 2011
- 13Barnes et al., Molecular Cell 2015
- 14Bernecky et al., Nature 2016
- 15Abdelkareem et al., Molecular Cell 2019
- 16Yin and Steitz, Science 2002
- 17Studier and Moffatt, Journal of Molecular Biology 1986
- 18Singh and Padgett, Nature Structural and Molecular Biology 2009
- 19Jonkers et al., eLife 2014
- 20Gout et al., PNAS 2013