Difference between revisions of "RsbR"

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==Original Articles==
 
==Original Articles==
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<pubmed>8002610,8682769,8682789, 17726680,10781545,15583165, 8824586,10329124,17158665, 9179850,8808936,15312768, 11244072,15342582,15378759, 12950928, 15466036, 9179850, 8955331, 18832644 ,17726680 ,17218307 20019076 21602359 23320651,21362065,20935101,22287516,22609918 </pubmed>
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<pubmed>8002610,8682769,8682789, 17726680,10781545,15583165, 8824586,10329124,17158665, 9179850,8808936,15312768, 11244072,15342582,15378759, 12950928, 15466036, 9179850, 8955331, 18832644 ,17726680 ,17218307 20019076 21602359 23320651,21362065,20935101,22287516,22609918 24599254 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:25, 8 March 2014

  • Description: activator of RsbT kinase activity, stressosome sensor protein
Gene name rsbR
Synonyms ycxR, rsbRA
Essential no
Product activator of RsbT kinase activity, stressosome sensor protein
Function control of SigB activity
Gene expression levels in SubtiExpress: rsbR
Interactions involving this protein in SubtInteract: RbsR
Metabolic function and regulation of this protein in SubtiPathways:
rsbR
MW, pI 30 kDa, 4.731
Gene length, protein length 822 bp, 274 aa
Immediate neighbours ndoA, rsbS
Sequences Protein DNA DNA_with_flanks
Genetic context
RsbR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RsbR expression.png















Categories containing this gene/protein

sigma factors and their control, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU04670

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • positive regulator of YtvA-dependent light activation of the SigB stress response PubMed
    • phosphorylated RsbR activates the kinase activity of RsbT PubMed
  • Protein family:

Extended information on the protein

  • Kinetic information:
  • Domains:
    • RsbRA is composed of an N-terminal nonheme globin domain and a highly conserved C-terminal STAS (Sulphate Transporter and AntiSigma factor antagonist) domain. The C-terminal STAS domain is the target of the serine/threonine-specific kinase RsbT (see below).
  • Modification: phosphorylation on Thr-171 and Thr-205 by RsbT PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 2BNL (N-terminal domain), 3VY9 (complete stressosome)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: constitutively expressed PubMed
  • Regulatory mechanism:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Marcel Jurk, Philipp Schramm, Peter Schmieder
The blue-light receptor YtvA from Bacillus subtilis is permanently incorporated into the stressosome independent of the illumination state.
Biochem Biophys Res Commun: 2013, 432(3);499-503
[PubMed:23416074] [WorldCat.org] [DOI] (I p)

Jon Marles-Wright, Richard J Lewis
The stressosome: molecular architecture of a signalling hub.
Biochem Soc Trans: 2010, 38(4);928-33
[PubMed:20658979] [WorldCat.org] [DOI] (I p)

Jon Marles-Wright, Richard J Lewis
The Bacillus subtilis stressosome: A signal integration and transduction hub.
Commun Integr Biol: 2008, 1(2);182-4
[PubMed:19704888] [WorldCat.org] [DOI] (I p)

Jan Pané-Farré, Richard J Lewis, Jörg Stülke
The RsbRST stress module in bacteria: a signalling system that may interact with different output modules.
J Mol Microbiol Biotechnol: 2005, 9(2);65-76
[PubMed:16319496] [WorldCat.org] [DOI] (P p)


Original Articles

Tatiana A Gaidenko, Chester W Price
Genetic evidence for a phosphorylation-independent signal transduction mechanism within the Bacillus subtilis stressosome.
PLoS One: 2014, 9(3);e90741
[PubMed:24599254] [WorldCat.org] [DOI] (I e)

Ulf W Liebal, Thomas Millat, Jon Marles-Wright, Richard J Lewis, Olaf Wolkenhauer
Simulations of stressosome activation emphasize allosteric interactions between RsbR and RsbT.
BMC Syst Biol: 2013, 7;3
[PubMed:23320651] [WorldCat.org] [DOI] (I e)

Tatiana A Gaidenko, Xiaomei Bie, Enoch P Baldwin, Chester W Price
Two surfaces of a conserved interdomain linker differentially affect output from the RST sensing module of the Bacillus subtilis stressosome.
J Bacteriol: 2012, 194(15);3913-21
[PubMed:22609918] [WorldCat.org] [DOI] (I p)

Jeroen B van der Steen, Marcela Avila-Pérez, Doreen Knippert, Angie Vreugdenhil, Pascal van Alphen, Klaas J Hellingwerf
Differentiation of function among the RsbR paralogs in the general stress response of Bacillus subtilis with regard to light perception.
J Bacteriol: 2012, 194(7);1708-16
[PubMed:22287516] [WorldCat.org] [DOI] (I p)

Tatiana A Gaidenko, Xiaomei Bie, Enoch P Baldwin, Chester W Price
Substitutions in the presumed sensing domain of the Bacillus subtilis stressosome affect its basal output but not response to environmental signals.
J Bacteriol: 2011, 193(14);3588-97
[PubMed:21602359] [WorldCat.org] [DOI] (I p)

Christine Eymann, Stephan Schulz, Katrin Gronau, Dörte Becher, Michael Hecker, Chester W Price
In vivo phosphorylation patterns of key stressosome proteins define a second feedback loop that limits activation of Bacillus subtilis σB.
Mol Microbiol: 2011, 80(3);798-810
[PubMed:21362065] [WorldCat.org] [DOI] (I p)

Luis Martinez, Adam Reeves, William Haldenwang
Stressosomes formed in Bacillus subtilis from the RsbR protein of Listeria monocytogenes allow σ(B) activation following exposure to either physical or nutritional stress.
J Bacteriol: 2010, 192(23);6279-86
[PubMed:20935101] [WorldCat.org] [DOI] (I p)

Adam Reeves, Luis Martinez, William Haldenwang
Expression of, and in vivo stressosome formation by, single members of the RsbR protein family in Bacillus subtilis.
Microbiology (Reading): 2010, 156(Pt 4);990-998
[PubMed:20019076] [WorldCat.org] [DOI] (I p)

Jon Marles-Wright, Tim Grant, Olivier Delumeau, Gijs van Duinen, Susan J Firbank, Peter J Lewis, James W Murray, Joseph A Newman, Maureen B Quin, Paul R Race, Alexis Rohou, Willem Tichelaar, Marin van Heel, Richard J Lewis
Molecular architecture of the "stressosome," a signal integration and transduction hub.
Science: 2008, 322(5898);92-6
[PubMed:18832644] [WorldCat.org] [DOI] (I p)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Adam Reeves, W G Haldenwang
Isolation and characterization of dominant mutations in the Bacillus subtilis stressosome components RsbR and RsbS.
J Bacteriol: 2007, 189(5);1531-41
[PubMed:17158665] [WorldCat.org] [DOI] (P p)

Shrin Kuo, Shuyu Zhang, Robyn L Woodbury, W G Haldenwang
Associations between Bacillus subtilis sigmaB regulators in cell extracts.
Microbiology (Reading): 2004, 150(Pt 12);4125-36
[PubMed:15583165] [WorldCat.org] [DOI] (P p)

Chien-Cheng Chen, Michael D Yudkin, Olivier Delumeau
Phosphorylation and RsbX-dependent dephosphorylation of RsbR in the RsbR-RsbS complex of Bacillus subtilis.
J Bacteriol: 2004, 186(20);6830-6
[PubMed:15466036] [WorldCat.org] [DOI] (P p)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
In vivo phosphorylation of partner switching regulators correlates with stress transmission in the environmental signaling pathway of Bacillus subtilis.
J Bacteriol: 2004, 186(18);6124-32
[PubMed:15342582] [WorldCat.org] [DOI] (P p)

Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis.
J Mol Biol: 2004, 341(1);135-50
[PubMed:15312768] [WorldCat.org] [DOI] (P p)

Chien-Cheng Chen, Richard J Lewis, Robin Harris, Michael D Yudkin, Olivier Delumeau
A supramolecular complex in the environmental stress signalling pathway of Bacillus subtilis.
Mol Microbiol: 2003, 49(6);1657-69
[PubMed:12950928] [WorldCat.org] [DOI] (P p)

S Zhang, J M Scott, W G Haldenwang
Loss of ribosomal protein L11 blocks stress activation of the Bacillus subtilis transcription factor sigma(B).
J Bacteriol: 2001, 183(7);2316-21
[PubMed:11244072] [WorldCat.org] [DOI] (P p)

J M Scott, J Ju, T Mitchell, W G Haldenwang
The Bacillus subtilis GTP binding protein obg and regulators of the sigma(B) stress response transcription factor cofractionate with ribosomes.
J Bacteriol: 2000, 182(10);2771-7
[PubMed:10781545] [WorldCat.org] [DOI] (P p)

T A Gaidenko, X Yang, Y M Lee, C W Price
Threonine phosphorylation of modulator protein RsbR governs its ability to regulate a serine kinase in the environmental stress signaling pathway of Bacillus subtilis.
J Mol Biol: 1999, 288(1);29-39
[PubMed:10329124] [WorldCat.org] [DOI] (P p)

S Akbar, C M Kang, T A Gaidenko, C W Price
Modulator protein RsbR regulates environmental signalling in the general stress pathway of Bacillus subtilis.
Mol Microbiol: 1997, 24(3);567-78
[PubMed:9179850] [WorldCat.org] [DOI] (P p)

U Voelker, A Voelker, W G Haldenwang
The yeast two-hybrid system detects interactions between Bacillus subtilis sigmaB regulators.
J Bacteriol: 1996, 178(23);7020-3
[PubMed:8955331] [WorldCat.org] [DOI] (P p)

X Yang, C M Kang, M S Brody, C W Price
Opposing pairs of serine protein kinases and phosphatases transmit signals of environmental stress to activate a bacterial transcription factor.
Genes Dev: 1996, 10(18);2265-75
[PubMed:8824586] [WorldCat.org] [DOI] (P p)

U Voelker, A Voelker, W G Haldenwang
Reactivation of the Bacillus subtilis anti-sigma B antagonist, RsbV, by stress- or starvation-induced phosphatase activities.
J Bacteriol: 1996, 178(18);5456-63
[PubMed:8808936] [WorldCat.org] [DOI] (P p)

C M Kang, M S Brody, S Akbar, X Yang, C W Price
Homologous pairs of regulatory proteins control activity of Bacillus subtilis transcription factor sigma(b) in response to environmental stress.
J Bacteriol: 1996, 178(13);3846-53
[PubMed:8682789] [WorldCat.org] [DOI] (P p)

A Dufour, U Voelker, A Voelker, W G Haldenwang
Relative levels and fractionation properties of Bacillus subtilis σ(B) and its regulators during balanced growth and stress.
J Bacteriol: 1996, 178(13);3701-9 sigma
[PubMed:8682769] [WorldCat.org] [DOI] (P p)

A A Wise, C W Price
Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sigma B in response to environmental signals.
J Bacteriol: 1995, 177(1);123-33
[PubMed:8002610] [WorldCat.org] [DOI] (P p)

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