Difference between revisions of "RsbS"

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scaffold protein of the [[stressosome]], anti-[[RsbT]]
  
 
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|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
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|style="background:#ABCDEF;" align="center"| '''Product''' || anti-[[RsbT]]
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|style="background:#ABCDEF;" align="center"| '''Product''' || scaffold protein of the [[stressosome]], anti-[[RsbT]]
 
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
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* '''Domains:'''  
 
* '''Domains:'''  
  
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* '''Modification:''' phosphorylation on Ser-59 [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], dephosphorylation by [[RsbX]] {{PubMed|21362065}}
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* '''Modification:''' phosphorylation on Ser-59 by [[RsbT]] [http://www.ncbi.nlm.nih.gov/sites/entrez/17218307 PubMed], dephosphorylation by [[RsbX]] {{PubMed|21362065}}
  
 
* '''Cofactor(s):'''
 
* '''Cofactor(s):'''
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rsbS_520237_520602_1 rsbS] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rsbS_520237_520602_1 rsbS] {{PubMed|22383849}}
  
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* '''Sigma factor:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed]
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed]
  
 
* '''Regulation:''' constitutively expressed {{PubMed|20019076}}  
 
* '''Regulation:''' constitutively expressed {{PubMed|20019076}}  
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==Original Articles==
 
==Original Articles==
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'''Additional publications:''' {{PubMed|21362065}}
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'''Additional publications:''' {{PubMed|23320651,21362065}}
 
<pubmed>8002610,8682769,9786195,8682789,10781545, 15583165,8824586,10329124,17158665, 21821766 16321960,10671474,8808936,15312768,11244072,15342582,,16321960, 8955331, 12950928, 15466036, 9179850, 18832644 ,17218307 20019076</pubmed>
 
<pubmed>8002610,8682769,9786195,8682789,10781545, 15583165,8824586,10329124,17158665, 21821766 16321960,10671474,8808936,15312768,11244072,15342582,,16321960, 8955331, 12950928, 15466036, 9179850, 18832644 ,17218307 20019076</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:19, 5 February 2013

scaffold protein of the stressosome, anti-RsbT

Gene name rsbS
Synonyms ycxS
Essential no
Product scaffold protein of the stressosome, anti-RsbT
Function control of SigB activity
Gene expression levels in SubtiExpress: rsbS
Interactions involving this protein in SubtInteract: RsbS
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 13 kDa, 4.14
Gene length, protein length 363 bp, 121 aa
Immediate neighbours rsbR, rsbT
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RsbS context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RsbS expression.png















Categories containing this gene/protein

sigma factors and their control, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU04680

Phenotypes of a mutant

Database entries

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

Additional information

  • A mutation was found in this gene after evolution under relaxed selection for sporulation PubMed


The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 3VY9 (complete stressosome)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation: constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews


Original Articles

Additional publications: PubMed

Christopher T Brown, Laura K Fishwick, Binna M Chokshi, Marissa A Cuff, Jay M Jackson, Travis Oglesby, Alison T Rioux, Enrique Rodriguez, Gregory S Stupp, Austin H Trupp, James S Woollcombe-Clarke, Tracy N Wright, William J Zaragoza, Jennifer C Drew, Eric W Triplett, Wayne L Nicholson
Whole-genome sequencing and phenotypic analysis of Bacillus subtilis mutants following evolution under conditions of relaxed selection for sporulation.
Appl Environ Microbiol: 2011, 77(19);6867-77
[PubMed:21821766] [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)

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)

Shuyu Zhang, Adam Reeves, Robyn L Woodbury, W G Haldenwang
Coexpression patterns of sigma(B) regulators in Bacillus subtilis affect sigma(B) inducibility.
J Bacteriol: 2005, 187(24);8520-5
[PubMed:16321960] [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)

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)

J M Scott, T Mitchell, W G Haldenwang
Stress triggers a process that limits activation of the Bacillus subtilis stress transcription factor sigma(B).
J Bacteriol: 2000, 182(5);1452-6
[PubMed:10671474] [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)

C M Kang, K Vijay, C W Price
Serine kinase activity of a Bacillus subtilis switch protein is required to transduce environmental stress signals but not to activate its target PP2C phosphatase.
Mol Microbiol: 1998, 30(1);189-96
[PubMed:9786195] [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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