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Journal Articles Nature Communications Year : 2016

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

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 reorganizes 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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Dates and versions

hal-03535654 , version 1 (19-01-2022)

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Michael Pilsl, Corinne Crucifix, Gabor Papai, Ferdinand Krupp, Robert Steinbauer, et al.. Structure of the initiation-competent RNA polymerase I and its implication for transcription. Nature Communications, 2016, 7 (1), pp.12126. ⟨10.1038/ncomms12126⟩. ⟨hal-03535654⟩
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