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Updated: Dec 5, 2025

Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach
Published on: March 12, 2017
Structural basis of Mfd-dependent transcription termination
Jing Shi1,2,3, Aijia Wen1, Minxing Zhao4
1Department of Biophysics, Zhejiang University School of Medicine, Hangzhou 310058, China.
Abstract:
Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite extensive studies, the molecular mechanism of Mfd-dependent transcription termination in bacteria remains unclear, with several long-standing puzzles. How Mfd is activated by stalled RNA polymerase (RNAP) and how activated Mfd translocates along the DNA are unknown. Here, we report the single-particle cryo-electron microscopy structures of T. thermophilus Mfd-RNAP complex with and without ATPγS. The structures reveal that Mfd undergoes profound conformational changes upon activation, contacts the RNAP β1 domain and its clamp, and pries open the RNAP clamp. These structures provide a foundation for future studies aimed at dissecting the precise mechanism of Mfd-dependent transcription termination and pave the way for rational drug design targeting Mfd for the purpose of tackling the antimicrobial resistance crisis.
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