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Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding
Toxin-antitoxin (TA) modules are pairs of genes essential for bacterial regulation upon environmental stresses. The mazEF module encodes the MazF toxin and its cognate MazE antitoxin. The highly dynamic MazE possesses an N-terminal DNA binding domain through which it can negatively regulate its own...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333400/ https://www.ncbi.nlm.nih.gov/pubmed/25564525 http://dx.doi.org/10.1093/nar/gku1352 |
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author | Zorzini, Valentina Buts, Lieven Schrank, Evelyne Sterckx, Yann G.J. Respondek, Michal Engelberg-Kulka, Hanna Loris, Remy Zangger, Klaus van Nuland, Nico A.J. |
author_facet | Zorzini, Valentina Buts, Lieven Schrank, Evelyne Sterckx, Yann G.J. Respondek, Michal Engelberg-Kulka, Hanna Loris, Remy Zangger, Klaus van Nuland, Nico A.J. |
author_sort | Zorzini, Valentina |
collection | PubMed |
description | Toxin-antitoxin (TA) modules are pairs of genes essential for bacterial regulation upon environmental stresses. The mazEF module encodes the MazF toxin and its cognate MazE antitoxin. The highly dynamic MazE possesses an N-terminal DNA binding domain through which it can negatively regulate its own promoter. Despite being one of the first TA systems studied, transcriptional regulation of Escherichia coli mazEF remains poorly understood. This paper presents the solution structure of C-terminal truncated E. coli MazE and a MazE-DNA model with a DNA palindrome sequence ∼10 bp upstream of the mazEF promoter. The work has led to a transcription regulator-DNA model, which has remained elusive thus far in the E. coli toxin–antitoxin family. Multiple complementary techniques including NMR, SAXS and ITC show that the long intrinsically disordered C-termini in MazE, required for MazF neutralization, does not affect the interactions between the antitoxin and its operator. Rather, the MazE C-terminus plays an important role in the MazF binding, which was found to increase the MazE affinity for the palindromic single site operator. |
format | Online Article Text |
id | pubmed-4333400 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-43334002015-03-18 Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding Zorzini, Valentina Buts, Lieven Schrank, Evelyne Sterckx, Yann G.J. Respondek, Michal Engelberg-Kulka, Hanna Loris, Remy Zangger, Klaus van Nuland, Nico A.J. Nucleic Acids Res Structural Biology Toxin-antitoxin (TA) modules are pairs of genes essential for bacterial regulation upon environmental stresses. The mazEF module encodes the MazF toxin and its cognate MazE antitoxin. The highly dynamic MazE possesses an N-terminal DNA binding domain through which it can negatively regulate its own promoter. Despite being one of the first TA systems studied, transcriptional regulation of Escherichia coli mazEF remains poorly understood. This paper presents the solution structure of C-terminal truncated E. coli MazE and a MazE-DNA model with a DNA palindrome sequence ∼10 bp upstream of the mazEF promoter. The work has led to a transcription regulator-DNA model, which has remained elusive thus far in the E. coli toxin–antitoxin family. Multiple complementary techniques including NMR, SAXS and ITC show that the long intrinsically disordered C-termini in MazE, required for MazF neutralization, does not affect the interactions between the antitoxin and its operator. Rather, the MazE C-terminus plays an important role in the MazF binding, which was found to increase the MazE affinity for the palindromic single site operator. Oxford University Press 2015-01-30 2015-01-06 /pmc/articles/PMC4333400/ /pubmed/25564525 http://dx.doi.org/10.1093/nar/gku1352 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Structural Biology Zorzini, Valentina Buts, Lieven Schrank, Evelyne Sterckx, Yann G.J. Respondek, Michal Engelberg-Kulka, Hanna Loris, Remy Zangger, Klaus van Nuland, Nico A.J. Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title | Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title_full | Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title_fullStr | Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title_full_unstemmed | Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title_short | Escherichia coli antitoxin MazE as transcription factor: insights into MazE-DNA binding |
title_sort | escherichia coli antitoxin maze as transcription factor: insights into maze-dna binding |
topic | Structural Biology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4333400/ https://www.ncbi.nlm.nih.gov/pubmed/25564525 http://dx.doi.org/10.1093/nar/gku1352 |
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