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Journal Article

Structural basis of RNA polymerase I transcription initiation.

MPS-Authors
/persons/resource/persons172942

Engel,  C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons203881

Gubbey,  T.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons200231

Neyer,  S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons203883

Sainsbury,  S.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons203885

Oberthür,  C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons134379

Bäjen,  C.
Department of Molecular Biology, MPI for Biophysical Chemistry, Max Planck Society;

/persons/resource/persons188847

Bernecky,  C.
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;

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Supplementary Material (public)

2416830_Suppl_1.pdf
(Supplementary material), 356KB

2416830_Suppl_2.mp4
(Supplementary material), 52MB

2416830_Suppl_3.mp4
(Supplementary material), 16MB

2416830_Suppl_4.pdf
(Supplementary material), 8MB

Citation

Engel, C., Gubbey, T., Neyer, S., Sainsbury, S., Oberthür, C., Bäjen, C., et al. (2017). Structural basis of RNA polymerase I transcription initiation. Cell, 169(1), 120-131. doi:10.1016/j.cell.2017.03.003.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-DD12-C
Abstract
Transcription initiation at the ribosomal RNA promoter requires RNA polymerase (Pol) I and the initiation factors Rrn3 and core factor (CF). Here, we combine X-ray crystallography and cryo-electron microscopy (cryo-EM) to obtain a molecular model for basal Pol I initiation. The three-subunit CF binds upstream promoter DNA, docks to the Pol I-Rrn3 complex, and loads DNA into the expanded active center cleft of the polymerase. DNA unwinding between the Pol I protrusion and clamp domains enables cleft contraction, resulting in an active Pol I conformation and RNA synthesis. Comparison with the Pol II system suggests that promoter specificity relies on a distinct "bendability" and "meltability" of the promoter sequence that enables contacts between initiation factors, DNA, and polymerase.