2013
DOI: 10.1016/j.bbrc.2013.02.025
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The blue-light receptor YtvA from Bacillus subtilis is permanently incorporated into the stressosome independent of the illumination state

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Cited by 19 publications
(26 citation statements)
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“…1). In contrast to the related RsbR co-antagonists, YtvA by itself does not appear capable of forming a stressosome with RsbS in vitro [37] and is only known to have a positive signaling role [11], [14], [15], [38]. Nonetheless, if its LOV domain were capable of redox as well as blue-light sensing, YtvA is a candidate for an S59-independent route of signaling, possibly detecting the secondary oxidative stress elicited by ethanol challenge [39].…”
Section: Resultsmentioning
confidence: 96%
“…1). In contrast to the related RsbR co-antagonists, YtvA by itself does not appear capable of forming a stressosome with RsbS in vitro [37] and is only known to have a positive signaling role [11], [14], [15], [38]. Nonetheless, if its LOV domain were capable of redox as well as blue-light sensing, YtvA is a candidate for an S59-independent route of signaling, possibly detecting the secondary oxidative stress elicited by ethanol challenge [39].…”
Section: Resultsmentioning
confidence: 96%
“…The results obtained were in general agreement with the earlier biochemical studies with respect to the number of RsbR proteins. In addition, it was shown that YtvA can form an integral part of stressosomes (see further below).…”
Section: The Environmental Branch Of the Gsr And The Functioning Of “mentioning
confidence: 99%
“…Nevertheless, YtvA does carry out its function as a blue‐light photoreceptor for the GSR as an integral part of the stressosomes . Using fluorescence microscopy, it was shown that YtvA localizes in spots that correspond to stressosomes in the presence of RsbRA, but that YtvA is diffusely localized with RsbRB as the only RsbR protein present .…”
Section: Ytva: a Blue‐light Photoreceptor Of The Gsrmentioning
confidence: 99%
“…Within Bacillus subtilis , a light sensing protein YtvA has been discovered (Losi et al, 2002; Avila-Perez et al, 2006, 2009). This protein is present in a stress sensing complex known as the stressosome which is composed of the proteins RsbR and its paralogs as well as RsbS and RsbT ( Figure 2 ; Gaidenko et al, 1999; Kim et al, 2004b; Hecker et al, 2007; Marles-Wright et al, 2008; Jurk et al, 2013). The stress signals are thought to be sensed by the protruding N- termini of these sensory proteins and are transduced into the core of the stressosome (Marles-Wright et al, 2008).…”
Section: Stresses Encountered In Foodmentioning
confidence: 99%