title: RNA polymerase I-Rrn3 complex at 4.8 Å resolution.
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.
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Christoph
authors.initials: C
authors.lastname: Engel
authors.affiliation: Max Planck Institute for Biochemistry, Department for Molecular Structural Biology, Am Klopferspitz 18, 82152 Martinsried, Germany.
authors.forename: Jürgen
authors.initials: J
authors.lastname: Plitzko
authors.affiliation: Max Planck Institute for Biophysical Chemistry, Department of Molecular Biology, Am Fassberg 11, 37077 Göttingen, Germany.
authors.forename: Patrick
authors.initials: P
authors.lastname: Cramer
mesh_terms: D020285:Cryoelectron Microscopy; D035463:Pol1 Transcription Initiation Complex Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D055503:Protein Multimerization; D012318:RNA Polymerase I / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism
chemical_list: D035463:Pol1 Transcription Initiation Complex Proteins; C101161:RRN3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D012318:RNA Polymerase I