Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Yan Han, Chunli Yan, Thi Hoang Duong Nguyen, Ashleigh J. Jackobel, Ivaylo Ivanov, Bruce A. Knutson*, Yuan He

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

49 Scopus citations


Transcription initiation by RNA Polymerase I (Pol I) depends on the Core Factor (CF) complex to recognize the upstream promoter and assemble into a Pre-Initiation Complex (PIC). Here, we solve a structure of Saccharomyces cerevisiae Pol I-CF-DNA to 3.8 Å resolution using single-particle cryo-electron microscopy. The structure reveals a bipartite architecture of Core Factor and its recognition of the promoter from 27 to 16. Core Factor’s intrinsic mobility correlates well with different conformational states of the Pol I cleft, in addition to the stabilization of either Rrn7 N-terminal domain near Pol I wall or the tandem winged helix domain of A49 at a partially overlapping location. Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in the Pol II PIC.

Original languageEnglish (US)
Article numbere27414
StatePublished - Jun 17 2017

ASJC Scopus subject areas

  • General Immunology and Microbiology
  • General Biochemistry, Genetics and Molecular Biology
  • General Neuroscience


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