6KJ6
cryo-EM structure of Escherichia coli Crl transcription activation complex
6KJ6 の概要
| エントリーDOI | 10.2210/pdb6kj6/pdb |
| EMDBエントリー | 0700 |
| 分子名称 | DNA-directed RNA polymerase subunit alpha, ZINC ION, MAGNESIUM ION, ... (11 entities in total) |
| 機能のキーワード | rna polymerase, escherichia coli, crl, transcription activation, transcription initiation, transcription regulator, sigma s, transcription |
| 由来する生物種 | Escherichia coli K-12 詳細 |
| タンパク質・核酸の鎖数 | 10 |
| 化学式量合計 | 478381.70 |
| 構造登録者 | |
| 主引用文献 | Xu, J.,Cui, K.,Shen, L.,Shi, J.,Li, L.,You, L.,Fang, C.,Zhao, G.,Feng, Y.,Yang, B.,Zhang, Y. Crl activates transcription by stabilizing active conformation of the master stress transcription initiation factor. Elife, 8:-, 2019 Cited by PubMed Abstract: σ is a master transcription initiation factor that protects bacterial cells from various harmful environmental stresses including antibiotic pressure. Although its mechanism remains unclear, it is known that full activation of σ-mediated transcription requires a σ-specific activator, Crl. In this study, we determined a 3.80 Å cryo-EM structure of an transcription activation complex ( Crl-TAC) comprising σ-RNA polymerase (σ-RNAP) holoenzyme, Crl, and a nucleic-acid scaffold. The structure reveals that Crl interacts with domain 2 of σ (σ) and the RNAP core enzyme, but does not contact promoter DNA. Results from subsequent hydrogen-deuterium exchange mass spectrometry (HDX-MS) indicate that Crl stabilizes key structural motifs within σ to promote the assembly of the σ-RNAP holoenzyme and also to facilitate formation of an RNA polymerase-promoter DNA open complex (RPo). Our study demonstrates a unique DNA contact-independent mechanism of transcription activation, thereby defining a previously unrecognized mode of transcription activation in cells. PubMed: 31846423DOI: 10.7554/eLife.50928 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.8 Å) |
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