Molecular Machinery
← RNA polymerase II

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

MeasuredVeloso 2014, opens the source in a new tabSingh 2009, opens the source in a new tab
MeasuredKimura 1999, opens the source in a new tab
EstimateKimura 1999, opens the source in a new tab
CalculatedVeloso 2014, opens the source in a new tabSingh 2009, opens the source in a new tabKimura 1999, opens the source in a new tab
EstimateBNID 109916, opens the source in a new tabBNID 111220, opens the source in a new tab
MeasuredSchwanhäusser 2011, opens the source in a new tabBNID 106378, opens the source in a new tab
CalculatedBNID 100667, opens the source in a new tabBNID 104208, opens the source in a new tab

Structures

  • 5C4X
    Yeast Pol II elongation complex with a complete bubble
    The complete transcription bubble in one entry: both DNA strands and the RNA, on all twelve subunits. X-ray diffraction, 4 Å.
  • 1I50
    Free yeast Pol II, clamp open
    The 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.
  • 1I6H
    Yeast Pol II elongation complex, clamp closed
    The 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.
  • 2E2H
    Pol II elongation complex with GTP in the active site
    Shows the substrate in the addition site, the state that closes the trigger loop over the nucleotide. X-ray diffraction, 3.95 Å.
  • 2VUM
    Pol II elongation complex inhibited by alpha-amanitin
    The 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.
  • 1K83
    Yeast Pol II with alpha-amanitin
    The first view of the amanitin site, next to the bridge helix. X-ray diffraction, 2.8 Å.
  • 5FLM
    Mammalian Pol II elongation complex
    The mammalian enzyme in the act of transcribing, for a species comparison with yeast. Electron microscopy, 3.4 Å.
  • 2O5I
    Bacterial RNA polymerase elongation complex
    The 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.
  • 2O5J
    Bacterial elongation complex with substrate analogue
    Same crystal form as 2O5I with substrate bound, so the trigger-loop folding step can be morphed. X-ray diffraction, 3 Å.
  • 2PPB
    Bacterial elongation complex with streptolydigin
    Shows an inactive pre-insertion substrate position, the state an antibiotic can freeze. X-ray diffraction, 3 Å.
  • 6RH3
    E. coli RNA polymerase elongation complex with CTP
    An E. coli elongation complex with clearly named template and non-template strands. Electron microscopy, 3.6 Å.
  • 1MSW
    T7 RNA polymerase elongation complex
    The single-subunit phage enzyme used for orthogonal expression. It shows how small a working polymerase can be. X-ray diffraction, 2.1 Å.

References

  1. 1Cramer et al., Science 2001
  2. 2Gnatt et al., Science 2001
  3. 3Bushnell and Kornberg, PNAS 2003
  4. 4Bushnell et al., PNAS 2002
  5. 5Brueckner and Cramer, Nature Structural and Molecular Biology 2008
  6. 6Wang et al., Cell 2006
  7. 7Vassylyev et al., Nature 2007, 448, 157-162
  8. 8Vassylyev et al., Nature 2007, 448, 163-168
  9. 9Sydow and Cramer, Current Opinion in Structural Biology 2009
  10. 10Sydow et al., Molecular Cell 2009
  11. 11Thomas et al., Cell 1998
  12. 12Cheung and Cramer, Nature 2011
  13. 13Barnes et al., Molecular Cell 2015
  14. 14Bernecky et al., Nature 2016
  15. 15Abdelkareem et al., Molecular Cell 2019
  16. 16Yin and Steitz, Science 2002
  17. 17Studier and Moffatt, Journal of Molecular Biology 1986
  18. 18Singh and Padgett, Nature Structural and Molecular Biology 2009
  19. 19Jonkers et al., eLife 2014
  20. 20Gout et al., PNAS 2013