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Journal Article

Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ

MPS-Authors
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Bürger,  Jörg
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Mielke,  Thorsten
Microscopy and Cryo-Electron Microscopy (Head: Thorsten Mielke), Scientific Service (Head: Christoph Krukenkamp), Max Planck Institute for Molecular Genetics, Max Planck Society;

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Said_2020.pdf
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Citation

Said, N., Hilal, T., Sunday, N. D., Khatri, A., Bürger, J., Mielke, T., et al. (2021). Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ. Science, 371(6524): eabd1673. doi:10.1126/science.abd1673.


Cite as: http://hdl.handle.net/21.11116/0000-0007-AD1D-7
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.