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-Structure paper
タイトル | Structural Basis for NusA Stabilized Transcriptional Pausing. |
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ジャーナル・号・ページ | Mol Cell, Vol. 69, Issue 5, Page 816-827.e4, Year 2018 |
掲載日 | 2018年3月1日 |
著者 | Xieyang Guo / Alexander G Myasnikov / James Chen / Corinne Crucifix / Gabor Papai / Maria Takacs / Patrick Schultz / Albert Weixlbaumer / |
PubMed 要旨 | Transcriptional pausing by RNA polymerases (RNAPs) is a key mechanism to regulate gene expression in all kingdoms of life and is a prerequisite for transcription termination. The essential bacterial ...Transcriptional pausing by RNA polymerases (RNAPs) is a key mechanism to regulate gene expression in all kingdoms of life and is a prerequisite for transcription termination. The essential bacterial transcription factor NusA stimulates both pausing and termination of transcription, thus playing a central role. Here, we report single-particle electron cryo-microscopy reconstructions of NusA bound to paused E. coli RNAP elongation complexes with and without a pause-enhancing hairpin in the RNA exit channel. The structures reveal four interactions between NusA and RNAP that suggest how NusA stimulates RNA folding, pausing, and termination. An asymmetric translocation intermediate of RNA and DNA converts the active site of the enzyme into an inactive state, providing a structural explanation for the inhibition of catalysis. Comparing RNAP at different stages of pausing provides insights on the dynamic nature of the process and the role of NusA as a regulatory factor. |
リンク | Mol Cell / PubMed:29499136 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 4.1 Å |
構造データ | |
化合物 | ChemComp-MG: ChemComp-ZN: |
由来 |
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キーワード | TRANSCRIPTION / RNA polymerase / Transcriptional pausing / his pause / NusA |