期刊
Nature Communications
卷 7, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12126
关键词
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资金
- Deutsche Forschungsgemeinschaft [SFB 960]
- Fondation pour la Recherche Medicale
- Institut National de la Sante et de la Recherche Medicale
- Centre National pour la Recherche Scientifique
- Strasbourg University
- Association pour la Recherche sur le Cancer
- Agence Nationale pour la Recherche
- Labex INRT
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
- INSTRUCT as part of the European Strategy Forum on Research Infrastructures (ESFRI)
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 angstrom 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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