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

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, N...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2021-01, Vol.371 (6524)
Main Authors: Said, Nelly, Hilal, Tarek, Sunday, Nicholas D, Khatri, Ajay, Bürger, Jörg, Mielke, Thorsten, Belogurov, Georgiy A, Loll, Bernhard, Sen, Ranjan, Artsimovitch, Irina, Wahl, Markus C
Format: Article
Language:English
Subjects:
Adenosine triphosphatase
Adenosine Triphosphatases - chemistry
Adenosine triphosphate
Cryoelectron Microscopy
Deactivation
Deoxyribonucleic acid
DNA
DNA-directed RNA polymerase
DNA-Directed RNA Polymerases - chemistry
Escherichia coli
Escherichia coli - genetics
Escherichia coli Proteins - chemistry
Inactivation
Microscopy
Multiprotein Complexes - chemistry
Peptide Elongation Factors - chemistry
Protein Conformation
Protein Transport
Rho Factor - chemistry
RNA polymerase
Structural Analysis (Linguistics)
Structural Analysis (Science)
Transcription Elongation, Genetic
Transcription Factors - chemistry
Transcriptional Elongation Factors - chemistry
Translocation
Zinc Fingers
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Summary: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abd1673