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Updated: Mar 17, 2026

Artificial RNA Polymerase II Elongation Complexes for Dissecting Co-transcriptional RNA Processing Events
Published on: May 13, 2019
RNA polymerase I-Rrn3 complex at 4.8 Å resolution.
Christoph Engel1, Jürgen Plitzko2, Patrick Cramer1
1Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany.
The initiation factor Rrn3 is essential for ribosomal DNA transcription by RNA polymerase I (Pol I). We determined the cryo-electron microscopy structure of the Pol I-Rrn3 complex, revealing its mechanism for activating Pol I for transcription initiation.
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Ribosomal DNA (rDNA) transcription is vital for cell growth and is primarily carried out by RNA polymerase I (Pol I).
- The initiation of Pol I transcription is a highly regulated process involving several factors, including the essential initiation factor Rrn3.
Purpose of the Study:
- To elucidate the structural basis of Rrn3's role in Pol I transcription initiation.
- To understand how Rrn3 interacts with Pol I and regulates its activity.
Main Methods:
- Cryo-electron microscopy (cryo-EM) was employed to determine the structure of the Pol I-Rrn3 complex.
- High-resolution structural analysis was performed at 4.8 Å.
Main Results:
- The cryo-EM structure reveals the atomic details of the Pol I-Rrn3 complex.
- Rrn3 binding induces a conformational change in Pol I, transitioning it from an inactive dimer to an active monomeric state.
- The structure provides mechanistic insights into Pol I-specific initiation.
Conclusions:
- Rrn3 acts as a key regulator, converting inactive Pol I into an initiation-competent form.
- The findings offer a structural understanding of Pol I-mediated rDNA transcription and its regulation.
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