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Structural basis of Rho-dependent transcription termination
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Journal Article
Structural basis of Rho-dependent transcription termination
2023
Overview
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 coli
1
–
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.
Structures presented in this study confirm decades of genetic and biochemical evidence for the mechanism of Rho-dependent termination in bacteria.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 38
/ 82
/ 82/80
/ 82/83
/ Acids
/ Adenosine Triphosphate - metabolism
/ DNA-Directed RNA Polymerases - chemistry
/ DNA-Directed RNA Polymerases - metabolism
/ DNA-Directed RNA Polymerases - ultrastructure
/ Escherichia coli - chemistry
/ Escherichia coli - enzymology
/ Escherichia coli - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - metabolism
/ Escherichia coli Proteins - ultrastructure
/ Humanities and Social Sciences
/ Ligands
/ RNA
/ Science
/ Transcription Factors - chemistry
/ Transcription Factors - metabolism
/ Transcription Factors - ultrastructure
