EMD-11725
Transcription termination complex IVa
EMD-11725
Single-particle4.2 Å
![EMD-11725](https://www.ebi.ac.uk/emdb/images/entry/EMD-11725/400_11725.gif)
Map released: 25/11/2020
Last modified: 01/05/2024
Sample Organism:
Escherichia coli,
synthetic construct
Sample: Transcription termination complex IVa
Fitted models: 7ade (Avg. Q-score: 0.235)
Deposition Authors: Said N
,
Hilal T
,
Loll B
,
Wahl CM,
Loll B
,
Wahl MC
Sample: Transcription termination complex IVa
Fitted models: 7ade (Avg. Q-score: 0.235)
Deposition Authors: Said N
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Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase rho.
Said N
,
Hilal T
,
Sunday ND
,
Khatri A,
Burger J
,
Mielke T
,
Belogurov GA
,
Loll B
,
Sen R
,
Artsimovitch I
,
Wahl MC
(2021) Science , 371
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(2021) Science , 371
Abstract:
Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.
Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state.