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-Structure paper
| タイトル | Structural basis of bacterial σ -mediated transcription reveals roles of the RNA polymerase zinc-binding domain. |
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| ジャーナル・号・ページ | EMBO J, Vol. 39, Issue 14, Page e104389, Year 2020 |
| 掲載日 | 2020年7月15日 |
著者 | Wei Shi / Wei Zhou / Baoyue Zhang / Shaojia Huang / Yanan Jiang / Abigail Schammel / Yangbo Hu / Bin Liu / ![]() |
| PubMed 要旨 | In bacteria, σ is the flagella-specific sigma factor that targets RNA polymerase (RNAP) to control the expression of flagella-related genes involving bacterial motility and chemotaxis. However, the ...In bacteria, σ is the flagella-specific sigma factor that targets RNA polymerase (RNAP) to control the expression of flagella-related genes involving bacterial motility and chemotaxis. However, the structural mechanism of σ -dependent promoter recognition remains uncharacterized. Here, we report cryo-EM structures of E. coli σ -dependent transcribing complexes on a complete flagella-specific promoter. These structures reveal how σ -RNAP recognizes promoter DNA through strong interactions with the -10 element, but weak contacts with the -35 element, to initiate transcription. In addition, we observed a distinct architecture in which the β' zinc-binding domain (ZBD) of RNAP stretches out from its canonical position to interact with the upstream non-template strand. Further in vitro and in vivo assays demonstrate that this interaction has the overall effect of facilitating closed-to-open isomerization of the RNAP-promoter complex by compensating for the weak interaction between σ4 and -35 element. This suggests that ZBD relocation may be a general mechanism employed by σ family factors to enhance transcription from promoters with weak σ4/-35 element interactions. |
リンク | EMBO J / PubMed:32484956 / PubMed Central |
| 手法 | EM (単粒子) |
| 解像度 | 3.86 - 3.91 Å |
| 構造データ | EMDB-20394, PDB-6pmi: EMDB-20395, PDB-6pmj: |
| 化合物 | ![]() ChemComp-ZN: ![]() ChemComp-MG: |
| 由来 |
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キーワード | TRANSCRIPTION / sigma28 / transcription initiation complex / RpoF / ZNR domain |
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