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Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR
The Escherichia coli MelR protein is a transcription activator that autoregulates its own promoter by repressing transcription initiation. Optimal repression requires MelR binding to a site that overlaps the melR transcription start point and to upstream sites. In this work, we have investigated the...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2377442/ https://www.ncbi.nlm.nih.gov/pubmed/18346968 http://dx.doi.org/10.1093/nar/gkn119 |
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author | Samarasinghe, Shivanthi El-Robh, Mohamed Samir Grainger, David C. Zhang, Wenke Soultanas, Panos Busby, Stephen J. W. |
author_facet | Samarasinghe, Shivanthi El-Robh, Mohamed Samir Grainger, David C. Zhang, Wenke Soultanas, Panos Busby, Stephen J. W. |
author_sort | Samarasinghe, Shivanthi |
collection | PubMed |
description | The Escherichia coli MelR protein is a transcription activator that autoregulates its own promoter by repressing transcription initiation. Optimal repression requires MelR binding to a site that overlaps the melR transcription start point and to upstream sites. In this work, we have investigated the different determinants needed for optimal repression and their spatial requirements. We show that repression requires a complex involving four DNA-bound MelR molecules, and that the global CRP regulator plays little or no role. |
format | Text |
id | pubmed-2377442 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-23774422008-05-14 Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR Samarasinghe, Shivanthi El-Robh, Mohamed Samir Grainger, David C. Zhang, Wenke Soultanas, Panos Busby, Stephen J. W. Nucleic Acids Res Molecular Biology The Escherichia coli MelR protein is a transcription activator that autoregulates its own promoter by repressing transcription initiation. Optimal repression requires MelR binding to a site that overlaps the melR transcription start point and to upstream sites. In this work, we have investigated the different determinants needed for optimal repression and their spatial requirements. We show that repression requires a complex involving four DNA-bound MelR molecules, and that the global CRP regulator plays little or no role. Oxford University Press 2008-05 2008-03-16 /pmc/articles/PMC2377442/ /pubmed/18346968 http://dx.doi.org/10.1093/nar/gkn119 Text en © 2008 The Author(s) http://creativecommons.org/licenses/by-nc/2.0/uk/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Molecular Biology Samarasinghe, Shivanthi El-Robh, Mohamed Samir Grainger, David C. Zhang, Wenke Soultanas, Panos Busby, Stephen J. W. Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title | Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title_full | Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title_fullStr | Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title_full_unstemmed | Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title_short | Autoregulation of the Escherichia coli melR promoter: repression involves four molecules of MelR |
title_sort | autoregulation of the escherichia coli melr promoter: repression involves four molecules of melr |
topic | Molecular Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2377442/ https://www.ncbi.nlm.nih.gov/pubmed/18346968 http://dx.doi.org/10.1093/nar/gkn119 |
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