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-Structure paper
タイトル | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 6420, Year 2020 |
掲載日 | 2020年12月18日 |
著者 | Timothy P Newing / Aaron J Oakley / Michael Miller / Catherine J Dawson / Simon H J Brown / James C Bouwer / Gökhan Tolun / Peter J Lewis / |
PubMed 要旨 | In bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram- ...In bacteria, transcription complexes stalled on DNA represent a major source of roadblocks for the DNA replication machinery that must be removed in order to prevent damaging collisions. Gram-positive bacteria contain a transcription factor HelD that is able to remove and recycle stalled complexes, but it was not known how it performed this function. Here, using single particle cryo-electron microscopy, we have determined the structures of Bacillus subtilis RNA polymerase (RNAP) elongation and HelD complexes, enabling analysis of the conformational changes that occur in RNAP driven by HelD interaction. HelD has a 2-armed structure which penetrates deep into the primary and secondary channels of RNA polymerase. One arm removes nucleic acids from the active site, and the other induces a large conformational change in the primary channel leading to removal and recycling of the stalled polymerase, representing a novel mechanism for recycling transcription complexes in bacteria. |
リンク | Nat Commun / PubMed:33339820 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.36 Å |
構造データ | EMDB-21920, PDB-6wvj: EMDB-21921, PDB-6wvk: |
化合物 | ChemComp-ZN: ChemComp-MG: |
由来 |
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キーワード | TRANSCRIPTION/DNA/RNA / DNA-DEPENDENT RNA POLYMERASE / TRANSCRIPTION / TRANSCRIPTION-DNA-RNA COMPLEX / RNA POLYMERASE / TRANSFERASE-HELD COMPLEX |