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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Autores principales:	Timothy P. Newing, Aaron J. Oakley, Michael Miller, Catherine J. Dawson, Simon H. J. Brown, James C. Bouwer, Gökhan Tolun, Peter J. Lewis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5ba51ba3f90b4dc994ae7757d1617c0b
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spelling	oai:doaj.org-article:5ba51ba3f90b4dc994ae7757d1617c0b2021-12-02T13:24:23ZMolecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD10.1038/s41467-020-20157-52041-1723https://doaj.org/article/5ba51ba3f90b4dc994ae7757d1617c0b2020-12-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-20157-5https://doaj.org/toc/2041-1723Gram-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.Timothy P. NewingAaron J. OakleyMichael MillerCatherine J. DawsonSimon H. J. BrownJames C. BouwerGökhan TolunPeter J. LewisNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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
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.
format	article
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
title	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_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_sort	molecular basis for rna polymerase-dependent transcription complex recycling by the helicase-like motor protein held
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/5ba51ba3f90b4dc994ae7757d1617c0b
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Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD

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