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Structural basis of Rho-dependent transcription termination

Vadim Molodtsov, Chengyuan Wang (), Emre Firlar, Jason T. Kaelber and Richard H. Ebright ()
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Vadim Molodtsov: Rutgers University
Chengyuan Wang: Rutgers University
Emre Firlar: Rutgers University
Jason T. Kaelber: Rutgers University
Richard H. Ebright: Rutgers University

Nature, 2023, vol. 614, issue 7947, 367-374

Abstract: Abstract Rho is a ring-shaped hexameric ATP-dependent molecular motor. Together with the transcription elongation factor NusG, Rho mediates factor-dependent transcription termination and transcription–translation-coupling quality control in Escherichia coli1–4. Here we report the preparation of complexes that are functional in factor-dependent transcription termination from Rho, NusG, RNA polymerase (RNAP), and synthetic nucleic acid scaffolds, and we report cryogenic electron microscopy structures of the complexes. The structures show that functional factor-dependent pre-termination complexes contain a closed-ring Rho hexamer; have RNA threaded through the central channel of Rho; have 60 nucleotides of RNA interacting sequence-specifically with the exterior of Rho and 6 nucleotides of RNA interacting sequence-specifically with the central channel of Rho; have Rho oriented relative to RNAP such that ATP-dependent translocation by Rho exerts mechanical force on RNAP; and have NusG bridging Rho and RNAP. The results explain five decades of research on Rho and provide a foundation for understanding Rho’s function.

Date: 2023
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DOI: 10.1038/s41586-022-05658-1

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