Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD
| Autor: | Catherine J. Dawson, James C. Bouwer, Aaron J. Oakley, Timothy P. Newing, Michael Miller, Gökhan Tolun, Simon H. J. Brown, Peter J. Lewis |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Models Molecular Transcription Elongation Genetic Transcription Genetic Science General Physics and Astronomy General Biochemistry Genetics and Molecular Biology Article 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Imaging Three-Dimensional Bacterial Proteins Transcription (biology) Cryoelectron microscopy RNA polymerase Transcription factor Polymerase Multidisciplinary biology DNA replication Helicase General Chemistry DNA-Directed RNA Polymerases Cell biology enzymes and coenzymes (carbohydrates) 030104 developmental biology chemistry Transcription preinitiation complex Enzyme mechanisms biology.protein bacteria Transcription 030217 neurology & neurosurgery DNA Bacillus subtilis Protein Binding |
| Zdroj: | Nature Communications, Vol 11, Iss 1, Pp 1-11 (2020) Nature Communications |
| ISSN: | 2041-1723 |
| Popis: | 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. Gram-positive bacteria contain a transcription factor HelD that is able to remove and recycle stalled transcription complexes. Here the authors provide mechanistic insights into this process by determining the cryo-EM structures of the Bacillus subtilis RNA polymerase (RNAP) elongation complex and the RNAP-HelD transcription recycling complex and propose a model of HelD catalysed transcription recycling. |
| Databáze: | OpenAIRE |
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