Structure of the initiation-competent RNA polymerase I and its implication for transcription

Michael Pilsl, Corinne Crucifix, Gabor Papai, Ferdinand Krupp, Robert Steinbauer, Joachim Griesenbeck, Philipp Milkereit, Herbert Tschochner () and Patrick Schultz ()
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Michael Pilsl: Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
Corinne Crucifix: IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
Gabor Papai: IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
Ferdinand Krupp: IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964
Robert Steinbauer: Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
Joachim Griesenbeck: Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
Philipp Milkereit: Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
Herbert Tschochner: Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie
Patrick Schultz: IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Eukaryotic RNA polymerase I (Pol I) is specialized in rRNA gene transcription synthesizing up to 60% of cellular RNA. High level rRNA production relies on efficient binding of initiation factors to the rRNA gene promoter and recruitment of Pol I complexes containing initiation factor Rrn3. Here, we determine the cryo-EM structure of the Pol I-Rrn3 complex at 7.5 Å resolution, and compare it with Rrn3-free monomeric and dimeric Pol I. We observe that Rrn3 contacts the Pol I A43/A14 stalk and subunits A190 and AC40, that association re-organizes the Rrn3 interaction interface, thereby preventing Pol I dimerization; and Rrn3-bound and monomeric Pol I differ from the dimeric enzyme in cleft opening, and localization of the A12.2 C-terminus in the active centre. Our findings thus support a dual role for Rrn3 in transcription initiation to stabilize a monomeric initiation competent Pol I and to drive pre-initiation complex formation.

Date: 2016
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DOI: 10.1038/ncomms12126

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