7F75
Cryo-EM structure of Spx-dependent transcription activation complex
7F75 の概要
| エントリーDOI | 10.2210/pdb7f75/pdb |
| EMDBエントリー | 31485 |
| 分子名称 | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit delta, MAGNESIUM ION, ... (12 entities in total) |
| 機能のキーワード | complex, transcription activator, stress, oxidated form, transcription, transcription-dna complex, transcription/dna |
| 由来する生物種 | Bacillus subtilis 詳細 |
| タンパク質・核酸の鎖数 | 12 |
| 化学式量合計 | 510067.69 |
| 構造登録者 | |
| 主引用文献 | Shi, J.,Li, F.,Wen, A.,Yu, L.,Wang, L.,Wang, F.,Jin, Y.,Jin, S.,Feng, Y.,Lin, W. Structural basis of transcription activation by the global regulator Spx. Nucleic Acids Res., 49:10756-10769, 2021 Cited by PubMed Abstract: Spx is a global transcriptional regulator in Gram-positive bacteria and has been inferred to efficiently activate transcription upon oxidative stress by engaging RNA polymerase (RNAP) and promoter DNA. However, the precise mechanism by which it interacts with RNAP and promoter DNA to initiate transcription remains obscure. Here, we report the cryo-EM structure of an intact Spx-dependent transcription activation complex (Spx-TAC) from Bacillus subtilis at 4.2 Å resolution. The structure traps Spx in an active conformation and defines key interactions accounting for Spx-dependent transcription activation. Strikingly, an oxidized Spx monomer engages RNAP by simultaneously interacting with the C-terminal domain of RNAP alpha subunit (αCTD) and σA. The interface between Spx and αCTD is distinct from those previously reported activators, indicating αCTD as a multiple target for the interaction between RNAP and various transcription activators. Notably, Spx specifically wraps the conserved -44 element of promoter DNA, thereby stabilizing Spx-TAC. Besides, Spx interacts extensively with σA through three different interfaces and promotes Spx-dependent transcription activation. Together, our structural and biochemical results provide a novel mechanistic framework for the regulation of bacterial transcription activation and shed new light on the physiological roles of the global Spx-family transcription factors. PubMed: 34530448DOI: 10.1093/nar/gkab790 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.2 Å) |
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