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-Structure paper
タイトル | CueR activates transcription through a DNA distortion mechanism. |
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ジャーナル・号・ページ | Nat Chem Biol, Vol. 17, Issue 1, Page 57-64, Year 2021 |
掲載日 | 2020年9月28日 |
![]() | Chengli Fang / Steven J Philips / Xiaoxian Wu / Kui Chen / Jing Shi / Liqiang Shen / Juncao Xu / Yu Feng / Thomas V O'Halloran / Yu Zhang / ![]() ![]() |
PubMed 要旨 | The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions ...The MerR-family transcription factors (TFs) are a large group of bacterial proteins responding to cellular metal ions and multiple antibiotics by binding within central RNA polymerase-binding regions of a promoter. While most TFs alter transcription through protein-protein interactions, MerR TFs are capable of reshaping promoter DNA. To address the question of which mechanism prevails, we determined two cryo-EM structures of transcription activation complexes (TAC) comprising Escherichia coli CueR (a prototype MerR TF), RNAP holoenzyme and promoter DNA. The structures reveal that this TF promotes productive promoter-polymerase association without canonical protein-protein contacts seen between other activator proteins and RNAP. Instead, CueR realigns the key promoter elements in the transcription activation complex by clamp-like protein-DNA interactions: these induce four distinct kinks that ultimately position the -10 element for formation of the transcription bubble. These structural and biochemical results provide strong support for the DNA distortion paradigm of allosteric transcriptional control by MerR TFs. |
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手法 | EM (単粒子) |
解像度 | 3.69 - 4.22 Å |
構造データ | EMDB-0874, PDB-6ldi: EMDB-30268, PDB-7c17: |
化合物 | ![]() ChemComp-ZN: ![]() ChemComp-MG: ![]() ChemComp-AG: |
由来 |
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![]() | TRANSCRIPTION (DNA to RNA) / RNA polymerase / CueR / transcription activation / TRANSCRIPTION |