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Structural basis of Q-dependent transcription antitermination.

Abstract：

: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 formation in the RNA exit channel. Because the RNA exit channel is conserved among all multisubunit RNAPs, it is likely to serve as an important contact site for regulators that modify the elongation properties of RNAP in other organisms, as well.

journal_name

Nat Commun

journal_title

Nature communications

authors

Shi J,Gao X,Tian T,Yu Z,Gao B,Wen A,You L,Chang S,Zhang X,Zhang Y,Feng Y

doi

10.1038/s41467-019-10958-8

subject

Has Abstract

pub_date

2019-07-02 00:00:00

pages

2925

issue

1

issn

2041-1723

pii

10.1038/s41467-019-10958-8

journal_volume

10

pub_type

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