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

被引：0

作者：

Michael Pilsl

Corinne Crucifix

Gabor Papai

Ferdinand Krupp

Robert Steinbauer

Joachim Griesenbeck

Philipp Milkereit

Herbert Tschochner

Patrick Schultz

机构：

[1] Universität Regensburg,Department of Integrated Structural Biology

[2] Biochemie-Zentrum Regensburg (BZR),undefined

[3] Institut für Biochemie,undefined

[4] Genetik und Mikrobiologie,undefined

[5] IGBMC (Institut de Génétique et de Biologie Moléculaire et Cellulaire) INSERM,undefined

[6] U964,undefined

[7] CNRS/Strasbourg University,undefined

[8] Present address: Sandoz GmbH,undefined

[9] Biochemiestraße 10,undefined

[10] 6250 Kundl,undefined

[11] Austria.,undefined

来源：

Nature Communications | / 7卷

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摘要：

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.

引用

共 134 条

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