Richard Ebright

Department of Chemistry and Chemical Biology
Rutgers University
Wednesday, Nov. 2, 2022
4:30pm
Taylor Auditorium, Frick Chemistry Laboratory
Host
Michael Hecht
Add to Calendar2022-11-02 16:30:002022-11-02 16:30:00Michael HechtTaylor Auditorium, Frick Chemistry Laboratory 15YYYY-MM-DD

Structural basis of transcription termination and transcription-translation-coupling quality control by Rho

Rho and NusG mediate factor-dependent transcription termination and transcription-translation-coupling quality control in Escherichia coli. Here, we report preparation of complexes functional in factor-dependent termination from RNA polymerase (RNAP), Rho, NusG, and synthetic nucleic-acid scaffolds, and we report cryo-EM structures of 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 nt of RNA interacting sequence-specifically with the exterior of Rho and 6 nt of RNA interacting sequence-specifically with the central channel of Rho, have Rho oriented relative to RNAP such that ATP-hydrolysis-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 function. 

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