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-Structure paper
Title | Structural mechanism of ATP-independent transcription initiation by RNA polymerase I. |
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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 |
Structure data | EMDB-8771, PDB-5w5y: EMDB-8772: EMDB-8773: EMDB-8774, PDB-5w64: EMDB-8775, PDB-5w65: EMDB-8776, PDB-5w66: EMDB-8777: |
Chemicals | ChemComp-ZN: |
Source |
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Keywords | TRANSCRIPTION / RNA Polymerase I Core Factor Transcription |