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Updated: Dec 5, 2025
12:12
Analysis of Termination of Transcription Using BrUTP-strand-specific Transcription Run-on TRO Approach
Published on: March 12, 2017
10.1K
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.
Nucleic Acids Research
|October 17, 2020
Summary
The Mfd protein
Area of Science:
- Molecular biology
- Microbiology
- Structural biology
Background:
- Mfd-dependent transcription termination is crucial for DNA repair and combating antibiotic resistance.
- The precise molecular mechanism of Mfd action remains incompletely understood.
- Key questions involve Mfd activation by stalled RNA polymerase (RNAP) and its DNA translocation.
Purpose of the Study:
- To elucidate the molecular mechanism of Mfd-dependent transcription termination.
- To provide structural insights into Mfd-RNAP interactions.
- To lay the groundwork for developing new antimicrobial strategies.
Main Methods:
- Single-particle cryo-electron microscopy (cryo-EM).
- Structural analysis of Thermus thermophilus Mfd-RNAP complex with and without ATPγS.
Main Results:
- Mfd undergoes significant conformational changes upon activation.
- Mfd interacts with the RNAP β1 domain and clamp.
- Mfd pries open the RNAP clamp structure.
Conclusions:
- The study reveals key structural details of Mfd activation and RNAP interaction.
- These findings offer a mechanistic basis for Mfd-dependent transcription termination.
- The structural data can inform drug design against antimicrobial resistance.
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