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DegS and RseP Homologous Proteases Are Involved in Singlet Oxygen Dependent Activation of RpoE in Rhodobacter sphaeroides
Authors:Aaron M Nuss  Fazal Adnan  Lennart Weber  Bork A Berghoff  Jens Glaeser  Gabriele Klug
Institution:1. Institute of Microbiology and Molecular Biology, Giessen University, Giessen, Germany.; 2. Department of Molecular Infection Biology, Helmholtz Centre for Infection Research, Braunschweig, Germany.; 3. Department of Cell and Molecular Biology, Biomedical Center, Uppsala University, Uppsala, Sweden.; Arizona State University, United States of America,
Abstract:Singlet oxygen (1O2) 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 1O2 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 1O2 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 1O2. Moreover, we revealed that the DegS and RseP homologs RSP_3242 and RSP_2710 contribute to 1O2 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 1O2 exposure in R. sphaeroides was extended.
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