|Title||Structural mechanism of ATP-independent transcription initiation by RNA polymerase I.|
|Journal, issue, pages||Elife, Vol. 6, Year 2017|
|Publish date||Jun 17, 2017|
|Authors||Yan Han / Chunli Yan / Thi Hoang Duong Nguyen / Ashleigh J Jackobel / Ivaylo Ivanov / Bruce A Knutson / Yuan He /|
|PubMed Abstract||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 ...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 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.|
|External links||Elife / PubMed:28623663 / PubMed Central|
|Methods||EM (single particle)|
|Resolution||3.7 - 6.9 Å|
|Keywords||Cryoelectron Microscopy / DNA, Fungal / Pol1 Transcription Initiation Complex Proteins / Protein Binding / RNA Polymerase I / RRN7 protein, S cerevisiae / Saccharomyces cerevisiae / Saccharomyces cerevisiae Proteins / Transcription Initiation, Genetic / TRANSCRIPTION / RNA Polymerase I Core Factor Transcription|
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