Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome.
The stressosome is a 1.8 MDa cytoplasmic complex that controls diverse bacterial signaling pathways. Its role is best understood in Bacillus subtilis, where it activates the σB transcription factor in response to a variety of sharp environmental challenges, including acid, ethanol, heat or salt stre...
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Public Library of Science (PLoS)
2014-01-01
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| Series: | PLoS ONE |
| Online Access: | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0090741&type=printable |
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| author | Tatiana A Gaidenko Chester W Price |
| author_facet | Tatiana A Gaidenko Chester W Price |
| author_sort | Tatiana A Gaidenko |
| collection | DOAJ |
| description | The stressosome is a 1.8 MDa cytoplasmic complex that controls diverse bacterial signaling pathways. Its role is best understood in Bacillus subtilis, where it activates the σB transcription factor in response to a variety of sharp environmental challenges, including acid, ethanol, heat or salt stress. However, details of the signaling mechanism within the stressosome remain uncertain. The core of the complex comprises one or more members of the RsbR co-antagonist family together with the RsbS antagonist protein, which binds the RsbT kinase in the absence of stress. As part of the response, RsbT first phosphorylates the RsbRA co-antagonist on T171 and then RsbS on S59; this latter event correlates with the stress-induced release of RsbT to activate downstream signaling. Here we examine the in vivo consequence of S59 phosphorylation in a model strain whose stressosome core is formed solely with the RsbRA co-antagonist and RsbS. A phosphorylation-deficient S59A substitution in RsbS blocked response to mild stress but had declining impact as stress increased: with strong ethanol challenge response with S59A was 60% as robust as with wild type RsbS. Genetic analysis narrowed this S59-independent activation to the stressosome and established that significant signaling still occurred in a strain bearing both the T171A and S59A substitutions. We infer that S59 phosphorylation increases signaling efficiency but is not essential, and that a second (or underlying) mechanism of signal transduction prevails in its absence. This interpretation nullifies models in which stressosome signaling is solely mediated by control of RsbT kinase activity toward S59. |
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| institution | DOAJ |
| issn | 1932-6203 |
| language | English |
| publishDate | 2014-01-01 |
| publisher | Public Library of Science (PLoS) |
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| spelling | doaj-art-e1251a57a38d4e5090a882c1f55dc3ac2025-08-20T03:11:55ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-0193e9074110.1371/journal.pone.0090741Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome.Tatiana A GaidenkoChester W PriceThe stressosome is a 1.8 MDa cytoplasmic complex that controls diverse bacterial signaling pathways. Its role is best understood in Bacillus subtilis, where it activates the σB transcription factor in response to a variety of sharp environmental challenges, including acid, ethanol, heat or salt stress. However, details of the signaling mechanism within the stressosome remain uncertain. The core of the complex comprises one or more members of the RsbR co-antagonist family together with the RsbS antagonist protein, which binds the RsbT kinase in the absence of stress. As part of the response, RsbT first phosphorylates the RsbRA co-antagonist on T171 and then RsbS on S59; this latter event correlates with the stress-induced release of RsbT to activate downstream signaling. Here we examine the in vivo consequence of S59 phosphorylation in a model strain whose stressosome core is formed solely with the RsbRA co-antagonist and RsbS. A phosphorylation-deficient S59A substitution in RsbS blocked response to mild stress but had declining impact as stress increased: with strong ethanol challenge response with S59A was 60% as robust as with wild type RsbS. Genetic analysis narrowed this S59-independent activation to the stressosome and established that significant signaling still occurred in a strain bearing both the T171A and S59A substitutions. We infer that S59 phosphorylation increases signaling efficiency but is not essential, and that a second (or underlying) mechanism of signal transduction prevails in its absence. This interpretation nullifies models in which stressosome signaling is solely mediated by control of RsbT kinase activity toward S59.https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0090741&type=printable |
| spellingShingle | Tatiana A Gaidenko Chester W Price Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. PLoS ONE |
| title | Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. |
| title_full | Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. |
| title_fullStr | Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. |
| title_full_unstemmed | Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. |
| title_short | Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome. |
| title_sort | genetic evidence for a phosphorylation independent signal transduction mechanism within the bacillus subtilis stressosome |
| url | https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0090741&type=printable |
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