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-Structure paper
タイトル | General transcription factor from Escherichia coli with a distinct mechanism of action. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 31, Issue 1, Page 141-149, Year 2024 |
掲載日 | 2024年1月4日 |
著者 | Nikita Vasilyev / Mengjie M J Liu / Vitaly Epshtein / Ilya Shamovsky / Evgeny Nudler / |
PubMed 要旨 | Gene expression in Escherichia coli is controlled by well-established mechanisms that activate or repress transcription. Here, we identify CedA as an unconventional transcription factor specifically ...Gene expression in Escherichia coli is controlled by well-established mechanisms that activate or repress transcription. Here, we identify CedA as an unconventional transcription factor specifically associated with the RNA polymerase (RNAP) σ holoenzyme. Structural and biochemical analysis of CedA bound to RNAP reveal that it bridges distant domains of β and σ subunits to stabilize an open-promoter complex. CedA does so without contacting DNA. We further show that cedA is strongly induced in response to amino acid starvation, oxidative stress and aminoglycosides. CedA provides a basal level of tolerance to these clinically relevant antibiotics, as well as to rifampicin and peroxide. Finally, we show that CedA modulates transcription of hundreds of bacterial genes, which explains its pleotropic effect on cell physiology and pathogenesis. |
リンク | Nat Struct Mol Biol / PubMed:38177674 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.76 Å |
構造データ | EMDB-29423, PDB-8ftd: |
化合物 | ChemComp-1N7: ChemComp-MG: ChemComp-ZN: |
由来 |
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キーワード | TRANSCRIPTION / TRANSFERASE/DNA / Escherichia coli / CedA / initiation complex / TRANSFERASE-DNA complex |