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-Structure paper
タイトル | Structural basis of Mfd-dependent transcription termination. |
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ジャーナル・号・ページ | Nucleic Acids Res, Vol. 48, Issue 20, Page 11762-11772, Year 2020 |
掲載日 | 2020年11月18日 |
著者 | Jing Shi / Aijia Wen / Minxing Zhao / Sha Jin / Linlin You / Yue Shi / Shuling Dong / Xiaoting Hua / Yu Zhang / Yu Feng / |
PubMed 要旨 | Mfd-dependent transcription termination plays an important role in transcription-coupled DNA repair, transcription-replication conflict resolution, and antimicrobial resistance development. Despite ...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. |
リンク | Nucleic Acids Res / PubMed:33068413 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 - 5.0 Å |
構造データ | EMDB-30117: CryoEM structure of Thermus thermophilus transcription-repair coupling complex in the absence of ATP-gamma-S EMDB-30118: CryoEM structure of Thermus thermophilus transcription-repair coupling complex in the presence of ATP-gamma-S EMDB-30119, PDB-6m6c: |
化合物 | ChemComp-ZN: ChemComp-MG: ChemComp-AGS: |
由来 |
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キーワード | TRANSCRIPTION / RNA polymerase / DNA repair / Mfd |