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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Main Authors: Timothy P. Newing, Aaron J. Oakley, Michael Miller, Catherine J. Dawson, Simon H. J. Brown, James C. Bouwer, Gökhan Tolun, Peter J. Lewis
Format: Article
Language:English
Published: Nature Portfolio 2020-12-01
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.
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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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