Threonine phosphorylation of modulator protein RsbR governs its ability to regulate a serine kinase in the environmental stress signaling pathway of Bacillus subtilis

Gaidenko, Tatiana A.; Yang, Xiaofeng; Lee, Young Moo; Price, Chester W.

doi:10.1006/jmbi.1999.2665

Cited by 75 publications

(146 citation statements)

References 37 publications

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“…Furthermore, phenotypes elicited by substitutions at the known or presumed sites of phosphorylation-threonines 171 and 205 of RsbRA or serine 59 of RsbS-support the hypothesis that modification of these proteins influences the transmission of environmental stress signals (2,12,16,18,30). However, the phenotypes of some RsbRA substitutions are significantly altered by the presence or absence of the other members of the RsbR coantagonist family (18).…”

Section: Separation and Identification Of Rsbra And Rsbs Isoformsmentioning

confidence: 58%

“…The RsbRA coantagonist and RsbS antagonist are known to be phosphorylated by the RsbT serine-threonine kinase in vitro (1,12,30). Furthermore, phenotypes elicited by substitutions at the known or presumed sites of phosphorylation-threonines 171 and 205 of RsbRA or serine 59 of RsbS-support the hypothesis that modification of these proteins influences the transmission of environmental stress signals (2,12,16,18,30).…”

Section: Separation and Identification Of Rsbra And Rsbs Isoformsmentioning

confidence: 76%

“…(C) RsbR coantagonist proteins share a carboxyl-terminal domain (shaded) with the smaller RsbS antagonist (1,25). In the RsbR family, this domain contains two conserved threonine (T) residues, and RsbT is known to phosphorylate RsbRA on T171 and T205 in vitro (12). In contrast, RsbS bears an aspartate (D) and a serine (S) at these corresponding positions.…”

Section: Methodsmentioning

confidence: 99%

“…This model further holds that the environmental signal is damped by the RsbX feedback phosphatase (24,27,30), whose expression is under B control (15). The biochemical and genetic evidence supporting this model includes a consideration of the phenotypes caused by alteration of the residues upon which RsbS and RsbRA are phosphorylated (2,12,16,18,30). However, it has yet to be established whether the in vivo phosphorylation state of the RsbR family members and RsbS do in fact change as a result of environmental stress.…”

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confidence: 99%

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In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

2004

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Exposure of bacteria to diverse growth-limiting stresses induces the synthesis of a common set of proteins which provide broad protection against future, potentially lethal stresses. Among Bacillus subtilis and its relatives, this general stress response is controlled by the B transcription factor. Signals of environmental and energy stress activate B through a multicomponent network that functions via a partner switching mechanism, in which protein-protein interactions are governed by serine and threonine phosphorylation. Here, we tested a central prediction of the current model for the environmental signaling branch of this network. We used isoelectric focusing and immunoblotting experiments to determine the in vivo phosphorylation states of the RsbRA and RsbS regulators, which act in concert to negatively control the RsbU environmental signaling phosphatase. As predicted by the model, the ratio of the phosphorylated to unphosphorylated forms of both RsbRA and RsbS increased in response to salt or ethanol stress. However, these two regulators differed substantially with regard to the extent of their phosphorylation under both steady-state and stress conditions, with RsbRA always the more highly modified. Mutant analysis showed that the RsbT kinase, which is required for environmental signaling, was also required for the in vivo phosphorylation of RsbRA and RsbS. Moreover, the T171A alteration of RsbRA, which blocks environmental signaling, also blocked in vivo phosphorylation of RsbRA and impeded phosphorylation of RsbS. These in vivo results corroborate previous genetic analyses and link the phosphorylated forms of RsbRA and RsbS to the active transmission of environmental stress signals.

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Section: Separation and Identification Of Rsbra And Rsbs Isoformsmentioning

confidence: 58%

Section: Separation and Identification Of Rsbra And Rsbs Isoformsmentioning

confidence: 76%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

2004

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“…In unstressed B. subtilis, RsbT is thought to be bound to an inhibitory protein (RsbS) in a high-molecular-mass complex (Ͼ10 6 Da) formed by members of a family of homologous proteins (RsbRA, -RB, -RC, and -RD) (10,20,21). The RsbR complex appears to modulate the interactions between RsbS and RsbT (1,2,10,14). In the absence of the RsbR proteins, RsbS is unable to inhibit RsbT's activation of RsbU (2).…”

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confidence: 99%

Coexpression Patterns of σ^BRegulators inBacillus subtilisAffect σ^BInducibility

et al. 2005

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RsbT is an essential component of the pathway that activates the Bacillus subtilisB transcription factor in response to physical stress. rsbT is located within an operon that includes the genes for its principal negative regulator (RsbS) and the stress pathway component that it activates (RsbU), as immediate upstream and downstream neighbors. In the current work we demonstrate that RsbT's ability to function is strongly influenced by coexpression with these adjoining genes. When rsbT is expressed at a site displaced from rsbS and rsbU, RsbT accumulates but it is unable to activate B following stress. RsbT activity is restored if rsbT is cotranscribed at the alternative site with the genes that normally abut it. Additionally, an rsbS allele whose product allows constitutively high RsbT-dependent B activity displays this activity in rsbS merodiploid strains only when cotranscribed with rsbT and is recessive to a wild-type rsbS allele only if the wild-type rsbS gene is not cotranscribed with an rsbT gene of its own. The data suggest that RsbS and RsbT are synthesized in equivalent amounts and interact coincidently with their synthesis to form stable regulatory complexes that maintain RsbT in a state from which it can be stress activated.

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High pressure effects step-wise altered protein expression inLactobacillus sanfranciscensis

et al. 2002

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In this study we investigated the cellular response to the application of high hydrostatic pressure. High pressure is increasingly used for food preservation. With high resolution 2-D electrophoresis we compared the protein patterns of atmospherically grown Lactobacillus sanfranciscensis with those pressure treated up to 200 MPa. We performed the comparative study by using overlapping immobilized pH gradients covering the pH range from 2.5 up to 12 in order to maximize the resolution for the detection of stress relevant proteins. For improved quantitative analysis, staining with SyproRuby was used in addition to silver staining. By computer aided image analysis we detected more than a dozen spots within the pH range from 3.5 to 9 that were more than two-fold increased or 50% decreased in their intensity upon high pressure treatment. Two of them (approx. values: pI 4.0 and 4.2, respectively; M(r) approximately 15 000) have almost identical matrix-assisted laser desorption/ionization-time of flight mass spectrometry spectra and were identified by liquid chromatography-tandem mass spectrometry as putative homologs/paralogs to cold shock proteins of Lactococcus lactis. Their expression is opposed (i.e. the more acidic one is repressed, while the other one is induced); this effect is maximal at 1 h, 150 MPa. It was further remarkable that by monitoring the barosensitivity of the cells within 25 MPa steps, we observed a differential pressure induction or repression of the detected proteins as well. For example one protein (approx. values: pI 4.2, M(r) approximately 15 000) shows a maximum induction after 1 h, 150 MPa while another one (pI 7.5, M(r) approximately 25 000) is maximally induced after 1 h, 50/75 MPa. This indicates a successive cell response and different signalling pathways for these responses.

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Threonine phosphorylation of modulator protein RsbR governs its ability to regulate a serine kinase in the environmental stress signaling pathway of Bacillus subtilis

Cited by 75 publications

References 37 publications

In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

Coexpression Patterns of σ^BRegulators inBacillus subtilisAffect σ^BInducibility

High pressure effects step-wise altered protein expression inLactobacillus sanfranciscensis

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Threonine phosphorylation of modulator protein RsbR governs its ability to regulate a serine kinase in the environmental stress signaling pathway of Bacillus subtilis

Cited by 75 publications

References 37 publications

In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

In Vivo Phosphorylation of Partner Switching Regulators Correlates with Stress Transmission in the Environmental Signaling Pathway ofBacillus subtilis

Coexpression Patterns of σBRegulators inBacillus subtilisAffect σBInducibility

High pressure effects step-wise altered protein expression inLactobacillus sanfranciscensis

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Coexpression Patterns of σ^BRegulators inBacillus subtilisAffect σ^BInducibility