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DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
Singlet oxygen ((1)O(2)) is the main agent of photooxidative stress and is generated by photosensitizers as (bacterio)chlorophylls. It leads to the damage of cellular macromolecules and therefore photosynthetic organisms have to mount an adaptive response to (1)O(2) formation. A major player of the...
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/PMC3818230/ https://www.ncbi.nlm.nih.gov/pubmed/24223961 http://dx.doi.org/10.1371/journal.pone.0079520 |
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author | Nuss, Aaron M. Adnan, Fazal Weber, Lennart Berghoff, Bork A. Glaeser, Jens Klug, Gabriele |
author_facet | Nuss, Aaron M. Adnan, Fazal Weber, Lennart Berghoff, Bork A. Glaeser, Jens Klug, Gabriele |
author_sort | Nuss, Aaron M. |
collection | PubMed |
description | Singlet oxygen ((1)O(2)) is the main agent of photooxidative stress and is generated by photosensitizers as (bacterio)chlorophylls. It leads to the damage of cellular macromolecules and therefore photosynthetic organisms have to mount an adaptive response to (1)O(2) formation. A major player of the photooxidative stress response in Rhodobacter sphaeroides is the alternative sigma factor RpoE, which is inactivated under non-stress conditions by its cognate anti-sigma factor ChrR. By using random mutagenesis we identified RSP_1090 to be required for full activation of the RpoE response under (1)O(2) stress, but not under organic peroxide stress. In this study we show that both RSP_1090 and RSP_1091 are required for full resistance towards (1)O(2). Moreover, we revealed that the DegS and RseP homologs RSP_3242 and RSP_2710 contribute to (1)O(2) resistance and promote ChrR proteolysis. The RpoE signaling pathway in R. sphaeroides is therefore highly similar to that of Escherichia coli, although very different anti-sigma factors control RpoE activity. Based on the acquired results, the current model for RpoE activation in response to (1)O(2) exposure in R. sphaeroides was extended. |
format | Online Article Text |
id | pubmed-3818230 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38182302013-11-09 DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides Nuss, Aaron M. Adnan, Fazal Weber, Lennart Berghoff, Bork A. Glaeser, Jens Klug, Gabriele PLoS One Research Article Singlet oxygen ((1)O(2)) is the main agent of photooxidative stress and is generated by photosensitizers as (bacterio)chlorophylls. It leads to the damage of cellular macromolecules and therefore photosynthetic organisms have to mount an adaptive response to (1)O(2) formation. A major player of the photooxidative stress response in Rhodobacter sphaeroides is the alternative sigma factor RpoE, which is inactivated under non-stress conditions by its cognate anti-sigma factor ChrR. By using random mutagenesis we identified RSP_1090 to be required for full activation of the RpoE response under (1)O(2) stress, but not under organic peroxide stress. In this study we show that both RSP_1090 and RSP_1091 are required for full resistance towards (1)O(2). Moreover, we revealed that the DegS and RseP homologs RSP_3242 and RSP_2710 contribute to (1)O(2) resistance and promote ChrR proteolysis. The RpoE signaling pathway in R. sphaeroides is therefore highly similar to that of Escherichia coli, although very different anti-sigma factors control RpoE activity. Based on the acquired results, the current model for RpoE activation in response to (1)O(2) exposure in R. sphaeroides was extended. Public Library of Science 2013-11-05 /pmc/articles/PMC3818230/ /pubmed/24223961 http://dx.doi.org/10.1371/journal.pone.0079520 Text en © 2013 Nuss 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 Nuss, Aaron M. Adnan, Fazal Weber, Lennart Berghoff, Bork A. Glaeser, Jens Klug, Gabriele DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides |
title | DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
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title_full | DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
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title_fullStr | DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
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title_full_unstemmed | DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
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title_short | DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
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title_sort | degs and rsep homologous proteases are involved in singlet oxygen dependent activation of rpoe in rhodobacter sphaeroides |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3818230/ https://www.ncbi.nlm.nih.gov/pubmed/24223961 http://dx.doi.org/10.1371/journal.pone.0079520 |
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