EMD-13714
CryoEM structure of E.coli RNA polymerase elongation complex bound to NusA and NusG (NusA and NusG elongation complex in less-swiveled conformation)
EMD-13714
Single-particle4.1 Å
![EMD-13714](https://www.ebi.ac.uk/emdb/images/entry/EMD-13714/400_13714.gif)
Map released: 23/03/2022
Last modified: 17/07/2024
Sample Organism:
Escherichia coli
Sample: NusA and NusG elongation complex in non-swiveled conformation
Fitted models: 7py6 (Avg. Q-score: 0.348)
Deposition Authors: Zhu C
,
Guo X
,
Weixlbaumer A
Sample: NusA and NusG elongation complex in non-swiveled conformation
Fitted models: 7py6 (Avg. Q-score: 0.348)
Deposition Authors: Zhu C
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Transcription factors modulate RNA polymerase conformational equilibrium.
Zhu C
,
Guo X
,
Dumas P,
Takacs M
,
Abdelkareem M,
Vanden Broeck A
,
Saint-Andre C,
Papai G
,
Crucifix C,
Ortiz J
,
Weixlbaumer A
(2022) Nat Commun , 13 , 1546 - 1546
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(2022) Nat Commun , 13 , 1546 - 1546
Abstract:
RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind RNAP simultaneously. Here we report cryo-EM reconstructions of Escherichia coli RNAP bound to NusG, or NusA, or both. RNAP conformational changes, referred to as swivelling, correlate with transcriptional pausing. NusA facilitates RNAP swivelling to further increase pausing, while NusG counteracts this role. Their structural effects are consistent with biochemical results on two categories of transcriptional pauses. In addition, the structures suggest a cooperative mechanism of NusA and NusG during Rho-mediated transcription termination. Our results provide a structural rationale for the stochastic nature of pausing and termination and how NusA and NusG can modulate it.
RNA polymerase (RNAP) frequently pauses during the transcription of DNA to RNA to regulate gene expression. Transcription factors NusA and NusG modulate pausing, have opposing roles, but can bind RNAP simultaneously. Here we report cryo-EM reconstructions of Escherichia coli RNAP bound to NusG, or NusA, or both. RNAP conformational changes, referred to as swivelling, correlate with transcriptional pausing. NusA facilitates RNAP swivelling to further increase pausing, while NusG counteracts this role. Their structural effects are consistent with biochemical results on two categories of transcriptional pauses. In addition, the structures suggest a cooperative mechanism of NusA and NusG during Rho-mediated transcription termination. Our results provide a structural rationale for the stochastic nature of pausing and termination and how NusA and NusG can modulate it.