Cargando…

Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD

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,...

Descripción completa

Detalles Bibliográficos
Autores principales: Newing, Timothy P., Oakley, Aaron J., Miller, Michael, Dawson, Catherine J., Brown, Simon H. J., Bouwer, James C., Tolun, Gökhan, Lewis, Peter J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749167/
https://www.ncbi.nlm.nih.gov/pubmed/33339820
http://dx.doi.org/10.1038/s41467-020-20157-5
_version_ 1783625258580836352
author Newing, Timothy P.
Oakley, Aaron J.
Miller, Michael
Dawson, Catherine J.
Brown, Simon H. J.
Bouwer, James C.
Tolun, Gökhan
Lewis, Peter J.
author_facet Newing, Timothy P.
Oakley, Aaron J.
Miller, Michael
Dawson, Catherine J.
Brown, Simon H. J.
Bouwer, James C.
Tolun, Gökhan
Lewis, Peter J.
author_sort Newing, Timothy P.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-7749167
institution National Center for Biotechnology Information
language English
publishDate 2020
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-77491672020-12-28 Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD Newing, Timothy P. Oakley, Aaron J. Miller, Michael Dawson, Catherine J. Brown, Simon H. J. Bouwer, James C. Tolun, Gökhan Lewis, Peter J. Nat Commun Article 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. Nature Publishing Group UK 2020-12-18 /pmc/articles/PMC7749167/ /pubmed/33339820 http://dx.doi.org/10.1038/s41467-020-20157-5 Text en © The Author(s) 2020 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Newing, Timothy P.
Oakley, Aaron J.
Miller, Michael
Dawson, Catherine J.
Brown, Simon H. J.
Bouwer, James C.
Tolun, Gökhan
Lewis, Peter J.
Molecular basis for RNA polymerase-dependent transcription complex recycling by the helicase-like motor protein HelD
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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7749167/
https://www.ncbi.nlm.nih.gov/pubmed/33339820
http://dx.doi.org/10.1038/s41467-020-20157-5
work_keys_str_mv AT newingtimothyp molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT oakleyaaronj molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT millermichael molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT dawsoncatherinej molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT brownsimonhj molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT bouwerjamesc molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT tolungokhan molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld
AT lewispeterj molecularbasisforrnapolymerasedependenttranscriptioncomplexrecyclingbythehelicaselikemotorproteinheld