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-Structure paper
タイトル | Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ. |
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ジャーナル・号・ページ | Science, Vol. 371, Issue 6524, Year 2021 |
掲載日 | 2021年1月1日 |
著者 | Nelly Said / Tarek Hilal / Nicholas D Sunday / Ajay Khatri / Jörg Bürger / Thorsten Mielke / Georgiy A Belogurov / Bernhard Loll / Ranjan Sen / Irina Artsimovitch / Markus C Wahl / |
PubMed 要旨 | Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ...Factor-dependent transcription termination mechanisms are poorly understood. We determined a series of cryo-electron microscopy structures portraying the hexameric adenosine triphosphatase (ATPase) ρ on a pathway to terminating NusA/NusG-modified elongation complexes. An open ρ ring contacts NusA, NusG, and multiple regions of RNA polymerase, trapping and locally unwinding proximal upstream DNA. NusA wedges into the ρ ring, initially sequestering RNA. Upon deflection of distal upstream DNA over the RNA polymerase zinc-binding domain, NusA rotates underneath one capping ρ subunit, which subsequently captures RNA. After detachment of NusG and clamp opening, RNA polymerase loses its grip on the RNA:DNA hybrid and is inactivated. Our structural and functional analyses suggest that ρ, and other termination factors across life, may use analogous strategies to allosterically trap transcription complexes in a moribund state. |
リンク | Science / PubMed:33243850 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.9 - 5.7 Å |
構造データ | EMDB-11087: Transcription termination complex 1 EMDB-11088, PDB-6z9q: EMDB-11089, PDB-6z9r: EMDB-11090: Transcription termination interdmediate complex 4 EMDB-11091, PDB-6z9t: EMDB-11722, PDB-7adb: EMDB-11723, PDB-7adc: EMDB-11724, PDB-7add: EMDB-11725, PDB-7ade: |
化合物 | ChemComp-BEF: ChemComp-ADP: ChemComp-MG: ChemComp-ZN: ChemComp-DG: ChemComp-HOH: ChemComp-DT: ChemComp-DA: |
由来 |
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キーワード | TRANSCRIPTION / Termination / Helicase / RNA Polymerase / Rho |