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Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities
The functions of several SOS regulated genes in Escherichia coli are still unknown, including dinQ. In this work we characterize dinQ and two small RNAs, agrA and agrB, with antisense complementarity to dinQ. Northern analysis revealed five dinQ transcripts, but only one transcript (+44) is actively...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567139/ https://www.ncbi.nlm.nih.gov/pubmed/23408903 http://dx.doi.org/10.1371/journal.pgen.1003260 |
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author | Weel-Sneve, Ragnhild Kristiansen, Knut Ivan Odsbu, Ingvild Dalhus, Bjørn Booth, James Rognes, Torbjørn Skarstad, Kirsten Bjørås, Magnar |
author_facet | Weel-Sneve, Ragnhild Kristiansen, Knut Ivan Odsbu, Ingvild Dalhus, Bjørn Booth, James Rognes, Torbjørn Skarstad, Kirsten Bjørås, Magnar |
author_sort | Weel-Sneve, Ragnhild |
collection | PubMed |
description | The functions of several SOS regulated genes in Escherichia coli are still unknown, including dinQ. In this work we characterize dinQ and two small RNAs, agrA and agrB, with antisense complementarity to dinQ. Northern analysis revealed five dinQ transcripts, but only one transcript (+44) is actively translated. The +44 dinQ transcript translates into a toxic single transmembrane peptide localized in the inner membrane. AgrB regulates dinQ RNA by RNA interference to counteract DinQ toxicity. Thus the dinQ-agr locus shows the classical features of a type I TA system and has many similarities to the tisB-istR locus. DinQ overexpression depolarizes the cell membrane and decreases the intracellular ATP concentration, demonstrating that DinQ can modulate membrane-dependent processes. Augmented DinQ strongly inhibits marker transfer by Hfr conjugation, indicating a role in recombination. Furthermore, DinQ affects transformation of nucleoid morphology in response to UV damage. We hypothesize that DinQ is a transmembrane peptide that modulates membrane-dependent activities such as nucleoid compaction and recombination. |
format | Online Article Text |
id | pubmed-3567139 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-35671392013-02-13 Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities Weel-Sneve, Ragnhild Kristiansen, Knut Ivan Odsbu, Ingvild Dalhus, Bjørn Booth, James Rognes, Torbjørn Skarstad, Kirsten Bjørås, Magnar PLoS Genet Research Article The functions of several SOS regulated genes in Escherichia coli are still unknown, including dinQ. In this work we characterize dinQ and two small RNAs, agrA and agrB, with antisense complementarity to dinQ. Northern analysis revealed five dinQ transcripts, but only one transcript (+44) is actively translated. The +44 dinQ transcript translates into a toxic single transmembrane peptide localized in the inner membrane. AgrB regulates dinQ RNA by RNA interference to counteract DinQ toxicity. Thus the dinQ-agr locus shows the classical features of a type I TA system and has many similarities to the tisB-istR locus. DinQ overexpression depolarizes the cell membrane and decreases the intracellular ATP concentration, demonstrating that DinQ can modulate membrane-dependent processes. Augmented DinQ strongly inhibits marker transfer by Hfr conjugation, indicating a role in recombination. Furthermore, DinQ affects transformation of nucleoid morphology in response to UV damage. We hypothesize that DinQ is a transmembrane peptide that modulates membrane-dependent activities such as nucleoid compaction and recombination. Public Library of Science 2013-02-07 /pmc/articles/PMC3567139/ /pubmed/23408903 http://dx.doi.org/10.1371/journal.pgen.1003260 Text en © 2013 Weel-Sneve et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Weel-Sneve, Ragnhild Kristiansen, Knut Ivan Odsbu, Ingvild Dalhus, Bjørn Booth, James Rognes, Torbjørn Skarstad, Kirsten Bjørås, Magnar Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title | Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title_full | Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title_fullStr | Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title_full_unstemmed | Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title_short | Single Transmembrane Peptide DinQ Modulates Membrane-Dependent Activities |
title_sort | single transmembrane peptide dinq modulates membrane-dependent activities |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3567139/ https://www.ncbi.nlm.nih.gov/pubmed/23408903 http://dx.doi.org/10.1371/journal.pgen.1003260 |
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