RNA polymerase I-Rrn3 complex at 4.8 Å resolution

Christoph Engel; Jürgen Plitzko; Patrick Cramer

doi:10.1038/ncomms12129

RNA polymerase I-Rrn3 complex at 4.8 Å resolution

Nat Commun. 2016 Jul 15:7:12129. doi: 10.1038/ncomms12129.

Authors

Christoph Engel¹, Jürgen Plitzko², Patrick Cramer¹

Affiliations

¹ Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany.
² Max Planck Institute for Biochemistry, Department for Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany.

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Cryoelectron Microscopy
Pol1 Transcription Initiation Complex Proteins / chemistry*
Pol1 Transcription Initiation Complex Proteins / genetics
Pol1 Transcription Initiation Complex Proteins / metabolism
Protein Multimerization
RNA Polymerase I / chemistry*
RNA Polymerase I / genetics
RNA Polymerase I / metabolism
Saccharomyces cerevisiae Proteins / chemistry*
Saccharomyces cerevisiae Proteins / metabolism

Substances

Pol1 Transcription Initiation Complex Proteins
RRN3 protein, S cerevisiae
Saccharomyces cerevisiae Proteins
RNA Polymerase I