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Nat Commun. 2016 Jul 15;7:12126. doi: 10.1038/ncomms12126.

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

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Universität Regensburg, Biochemie-Zentrum Regensburg (BZR), Institut für Biochemie, Genetik und Mikrobiologie, Lehrstuhl Biochemie III, 93053 Regensburg, Germany.
Department of Integrated Structural Biology, IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM, U964; CNRS/Strasbourg University, UMR7104 1, rue Laurent Fries, BP10142, 67404 Illkirch, France.


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.

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