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TitleStructure of the initiation-competent RNA polymerase I and its implication for transcription.
Journal, issue, pagesNat Commun, Vol. 7, Page 12126, Year 2016
Publish dateJul 15, 2016
AuthorsMichael Pilsl / Corinne Crucifix / Gabor Papai / Ferdinand Krupp / Robert Steinbauer / Joachim Griesenbeck / Philipp Milkereit / Herbert Tschochner / Patrick Schultz /
PubMed AbstractEukaryotic 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 ...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.
External linksNat Commun / PubMed:27418187 / PubMed Central
MethodsEM (single particle)
Resolution7.5 Å
Structure data

EMDB-3443:
Electron cryo-microscopy of the yeast RNA polymerase I - Rrn3 complex at 7.5A resolution
Method: EM (single particle) / Resolution: 7.5 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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