RNA polymerase I–Rrn3 complex at 4.8 Å resolution

Christoph Engel, Jürgen Plitzko and Patrick Cramer ()
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Christoph Engel: Max Planck Institute for Biophysical Chemistry
Jürgen Plitzko: Max Planck Institute for Biochemistry
Patrick Cramer: Max Planck Institute for Biophysical Chemistry

Nature Communications, 2016, vol. 7, issue 1, 1-5

Abstract: 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.

Date: 2016
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12129

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DOI: 10.1038/ncomms12129

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