EMD-11088
Transcription termination intermediate complex 2
EMD-11088
Single-particle5.7 Å
![EMD-11088](https://www.ebi.ac.uk/emdb/images/entry/EMD-11088/400_11088.gif)
Map released: 13/01/2021
Last modified: 28/07/2021
Sample Organism:
Escherichia coli
Sample: Transcription termination complex
Deposition Authors: Said N, Hilal T, Buerger J, Mielke T, Loll B, Wahl MC
Sample: Transcription termination complex
Deposition Authors: Said N, Hilal T, Buerger J, Mielke T, Loll B, Wahl MC
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.