論文 - 詳細
| RRC ID | 66169 |
|---|---|
| 著者 | Said N, Hilal T, Sunday ND, Khatri A, Bürger J, Mielke T, Belogurov GA, Loll B, Sen R, Artsimovitch I, Wahl MC. |
| タイトル | Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ. |
| ジャーナル | Science |
| Abstract |
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. |
| 巻・号 | 371(6524) |
| 公開日 | 2021-1-1 |
| DOI | 10.1126/science.abd1673 |
| PII | science.abd1673 |
| PMID | 33243850 |
| PMC | PMC7864586 |
| MeSH | Adenosine Triphosphatases / chemistry* Cryoelectron Microscopy DNA-Directed RNA Polymerases / chemistry* Escherichia coli / genetics* Escherichia coli Proteins / chemistry Multiprotein Complexes / chemistry Peptide Elongation Factors / chemistry Protein Conformation Protein Transport Rho Factor / chemistry* Transcription Elongation, Genetic* Transcription Factors / chemistry Transcriptional Elongation Factors / chemistry Zinc Fingers |
| IF | 41.846 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 42 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 原核生物(大腸菌) | |