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Journal Article

RNA polymerase I-Rrn3 complex at 4.8 Å resolution.

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

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

Fulltext (public)

2316548.pdf
(Publisher version), 2MB

Supplementary Material (public)

2316548_Suppl.pdf
(Supplementary material), 532KB

Citation

Engel, C., Plitzko, J., & Cramer, P. (2016). RNA polymerase I-Rrn3 complex at 4.8 Å resolution. Nature Communications, 7: 12129. doi:10.1038/ncomms12129.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-07DB-8
Abstract
Transcription of ribosomal DNA by RNA polymerase I (Pol I) requires the initiation factor Rrn3. Here we report the cryo-EM structure of the Pol I-Rrn3 complex at 4.8 Å resolution. The structure reveals how Rrn3 binding converts an inactive Pol I dimer into an initiation-competent monomeric complex and provides insights into the mechanisms of Pol I-specific initiation and regulation.