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The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage
During transcription elongation, bacterial RNA polymerase (RNAP) can pause, backtrack or stall when transcribing template DNA. Stalled transcription elongation complexes at sites of bulky lesions can be rescued by the transcription terminator Mfd. The molecular mechanisms of Mfd recruitment to trans...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5910403/ https://www.ncbi.nlm.nih.gov/pubmed/29679003 http://dx.doi.org/10.1038/s41467-018-03790-z |
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author | Ho, Han N. van Oijen, Antoine M. Ghodke, Harshad |
author_facet | Ho, Han N. van Oijen, Antoine M. Ghodke, Harshad |
author_sort | Ho, Han N. |
collection | PubMed |
description | During transcription elongation, bacterial RNA polymerase (RNAP) can pause, backtrack or stall when transcribing template DNA. Stalled transcription elongation complexes at sites of bulky lesions can be rescued by the transcription terminator Mfd. The molecular mechanisms of Mfd recruitment to transcription complexes in vivo remain to be elucidated, however. Using single-molecule live-cell imaging, we show that Mfd associates with elongation transcription complexes even in the absence of exogenous genotoxic stresses. This interaction requires an intact RNA polymerase-interacting domain of Mfd. In the presence of drugs that stall RNAP, we find that Mfd associates pervasively with RNAP. The residence time of Mfd foci reduces from 30 to 18 s in the presence of endogenous UvrA, suggesting that UvrA promotes the resolution of Mfd-RNAP complexes on DNA. Our results reveal that RNAP is frequently rescued by Mfd during normal growth and highlight a ubiquitous house-keeping role for Mfd in regulating transcription elongation. |
format | Online Article Text |
id | pubmed-5910403 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-59104032018-04-23 The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage Ho, Han N. van Oijen, Antoine M. Ghodke, Harshad Nat Commun Article During transcription elongation, bacterial RNA polymerase (RNAP) can pause, backtrack or stall when transcribing template DNA. Stalled transcription elongation complexes at sites of bulky lesions can be rescued by the transcription terminator Mfd. The molecular mechanisms of Mfd recruitment to transcription complexes in vivo remain to be elucidated, however. Using single-molecule live-cell imaging, we show that Mfd associates with elongation transcription complexes even in the absence of exogenous genotoxic stresses. This interaction requires an intact RNA polymerase-interacting domain of Mfd. In the presence of drugs that stall RNAP, we find that Mfd associates pervasively with RNAP. The residence time of Mfd foci reduces from 30 to 18 s in the presence of endogenous UvrA, suggesting that UvrA promotes the resolution of Mfd-RNAP complexes on DNA. Our results reveal that RNAP is frequently rescued by Mfd during normal growth and highlight a ubiquitous house-keeping role for Mfd in regulating transcription elongation. Nature Publishing Group UK 2018-04-20 /pmc/articles/PMC5910403/ /pubmed/29679003 http://dx.doi.org/10.1038/s41467-018-03790-z Text en © The Author(s) 2018 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 Ho, Han N. van Oijen, Antoine M. Ghodke, Harshad The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title | The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title_full | The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title_fullStr | The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title_full_unstemmed | The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title_short | The transcription-repair coupling factor Mfd associates with RNA polymerase in the absence of exogenous damage |
title_sort | transcription-repair coupling factor mfd associates with rna polymerase in the absence of exogenous damage |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5910403/ https://www.ncbi.nlm.nih.gov/pubmed/29679003 http://dx.doi.org/10.1038/s41467-018-03790-z |
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