2014
DOI: 10.1371/journal.pone.0090741
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Genetic Evidence for a Phosphorylation-Independent Signal Transduction Mechanism within the Bacillus subtilis Stressosome

Abstract: 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 prote… Show more

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Cited by 9 publications
(15 citation statements)
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“…Therefore, whatever the transduced signal may be, the system seems unrelated to classical bacterial phosphorylation relays. Thus, a phosphorylation‐independent conformational change or binding/unbinding to the membrane itself may propagate the transduced signal as in other systems (Gaidenko and Price, ). These putative two forms (DrpB On and DrpB Off ) are represented in the figure as quadrangular and oval forms.…”
Section: Discussionmentioning
confidence: 99%
“…Therefore, whatever the transduced signal may be, the system seems unrelated to classical bacterial phosphorylation relays. Thus, a phosphorylation‐independent conformational change or binding/unbinding to the membrane itself may propagate the transduced signal as in other systems (Gaidenko and Price, ). These putative two forms (DrpB On and DrpB Off ) are represented in the figure as quadrangular and oval forms.…”
Section: Discussionmentioning
confidence: 99%
“…As phosphorylation of both RsbR and RsbS was absolutely required for activation of the B. subtilis Rsb signaling pathway (Gaidenko & Price, 2014; Kim et al, 2004a), these studies suggest that Vb RsbR controls O 2 -dependent stressosome signaling in V. brasiliensis (Figure 13). These data also suggest that the conformational changes that occur in Vb RsbR upon O 2 association/dissociation are sufficient for signal propagation to multiple binding partners (Jia et al, 2016).…”
Section: Stressosome-related Gcs Proteinsmentioning
confidence: 89%
“…The non-heme globin maintains the sensor globin structure, but mutations within the globin heme pocket (including mutation of the proximal histidine) yielded a protein with a sensor globin fold that is unable to bind heme (Murray et al, 2005). The stressosome was demonstrated to be an ~1.8 MDa complex in B. subtilis formed by RsbR, RsbS (STAS domain that makes protein-protein interactions with the RsbR STAS domain), and RsbT (kinase, phosphorylates RsbR/RsbS) that senses environmental stress and, through a phosphorylation cascade involving additional rsb proteins, eventually resulting in activation of σ B and transcription of over 150 genes (Eymann et al, 2011; Gaidenko & Price, 2014; Kim, Gaidenko, & Price, 2004a, 2004b; Marles-Wright et al, 2008; Price et al, 2001). However, the ligand(s) that bind and activate the B. subtilis non-heme globin-containing RsbR are unknown.…”
Section: Stressosome-related Gcs Proteinsmentioning
confidence: 99%
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“…Phosphorylation of stressosome proteins is critical for the release of (the kinase) RsbT and the initiation of the GSR , although there may also be a phosphorylation‐independent way to release RsbT . RsbS contains a single serine residue that can be phosphorylated by RsbT: Ser59 .…”
Section: The Environmental Branch Of the Gsr And The Functioning Of “mentioning
confidence: 99%