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Structural basis of Q-dependent transcription antitermination.

Nat Commun. 2019-07; 
Shi J, Gao X, Tian T, Yu Z, Gao B, Wen A, You L, Chang S, Zhang X, Zhang Y, Feng Y.
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Peptide Synthesis Equilibrium fluorescence polarization assays of 21Q-FTH interaction were performed analogously to fluorescence polarization assay of 21Q-QBE interaction, using 0–100 μΜ 21Q or 21Q derivative and 0.1 μM N-terminal 5-FAM-labeled peptide (TPEEKLLRAIFGEK, GenScript, Inc.). Get A Quote

摘要

Bacteriophage Q protein engages σ-dependent paused RNA polymerase (RNAP) by binding to a DNA site embedded in late gene promoter and renders RNAP resistant to termination signals. Here, we report a single-particle cryo-electron microscopy (cryo-EM) structure of an intact Q-engaged arrested complex. The structure reveals key interactions responsible for σ-dependent pause, Q engagement, and Q-mediated transcription antitermination. The structure shows that two Q protomers (QI and QII) bind to a direct-repeat DNA site and contact distinct elements of the RNA exit channel. Notably, QI forms a narrow ring inside the RNA exit channel and renders RNAP resistant to termination signals by prohibiting RNA hairpin forma... More

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