Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD
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 t...
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Nature Portfolio
2020-12-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-20157-5 |
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author | Timothy P. Newing Aaron J. Oakley Michael Miller Catherine J. Dawson Simon H. J. Brown James C. Bouwer Gökhan Tolun Peter J. Lewis |
author_facet | Timothy P. Newing Aaron J. Oakley Michael Miller Catherine J. Dawson Simon H. J. Brown James C. Bouwer Gökhan Tolun Peter J. Lewis |
author_sort | Timothy P. Newing |
collection | DOAJ |
description | 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. |
first_indexed | 2024-12-17T20:30:25Z |
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id | doaj.art-5ba51ba3f90b4dc994ae7757d1617c0b |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-17T20:30:25Z |
publishDate | 2020-12-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-5ba51ba3f90b4dc994ae7757d1617c0b2022-12-21T21:33:36ZengNature PortfolioNature Communications2041-17232020-12-0111111110.1038/s41467-020-20157-5Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelDTimothy P. Newing0Aaron J. Oakley1Michael Miller2Catherine J. Dawson3Simon H. J. Brown4James C. Bouwer5Gökhan Tolun6Peter J. Lewis7Molecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research InstituteMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research InstituteSchool of Environmental and Life Sciences, University of NewcastleSchool of Environmental and Life Sciences, University of NewcastleMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research InstituteMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research InstituteMolecular Horizons and School of Chemistry and Molecular Bioscience, University of Wollongong, and Illawarra Health and Medical Research InstituteSchool of Environmental and Life Sciences, University of NewcastleGram-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.https://doi.org/10.1038/s41467-020-20157-5 |
spellingShingle | Timothy P. Newing Aaron J. Oakley Michael Miller Catherine J. Dawson Simon H. J. Brown James C. Bouwer Gökhan Tolun Peter J. Lewis Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD Nature Communications |
title | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD |
title_full | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD |
title_fullStr | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD |
title_full_unstemmed | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD |
title_short | Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD |
title_sort | molecular basis for rna polymerase dependent transcription complex recycling by the helicase like motor protein held |
url | https://doi.org/10.1038/s41467-020-20157-5 |
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