Difference between revisions of "RsbR"

From SubtiWiki
Jump to: navigation, search
Line 1: Line 1:
 +
* '''Description:''' activator of [[RsbT]] kinase activity, [[stressosome]] sensor protein
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
Line 9: Line 10:
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|style="background:#ABCDEF;" align="center"| '''Essential''' || no  
 
|-
 
|-
−
|style="background:#ABCDEF;" align="center"| '''Product''' || activator of [[RsbT]] kinase activity  
+
|style="background:#ABCDEF;" align="center"| '''Product''' || activator of [[RsbT]] kinase activity, [[stressosome]] sensor protein
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
 
|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
Line 70: Line 71:
 
* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
 
** positive regulator of [[YtvA]]-dependent light activation of the [[SigB]] stress response {{PubMed|22287516}}
 
** positive regulator of [[YtvA]]-dependent light activation of the [[SigB]] stress response {{PubMed|22287516}}
 +
** phosphorylated [[RsbR]] activates the kinase activity of [[RsbT]] {{PubMed|23320651}}
  
 
* '''Protein family:'''
 
* '''Protein family:'''
Line 79: Line 81:
 
* '''Kinetic information:'''
 
* '''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).
+
* '''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|21362065}}
 
* '''Modification:''' phosphorylation on Thr-171 and Thr-205 by [[RsbT]] {{PubMed|21362065}}
Line 89: Line 92:
 
* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
 
** [[RsbX]]-[[RsbR]] {{PubMed|15466036}}
 
** [[RsbX]]-[[RsbR]] {{PubMed|15466036}}
−
** [[RsbR]]-[[RsbT]] {{PubMed|21362065}},  [[RsbR]]-[[RsbS]]
+
** [[RsbR]]-[[RsbT]] {{PubMed|21362065}}
 +
** [[RsbR]]-[[RsbS]]
 
** component of the [[stressosome]]
 
** component of the [[stressosome]]
  

Revision as of 12:32, 5 February 2013

  • 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:
Stress
MW, pI 30 kDa, 4.731
Gene length, protein length 822 bp, 274 aa
Immediate neighbours ndoA, rsbS
Get the DNA and protein sequences
(Barbe et al., 2009)
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

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
  • Cofactor(s):
  • 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:
  • 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

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

Additional publications: PubMed

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)

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)

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)

Retrieved from "https://subtiwiki.uni-goettingen.de/wiki//index.php?title=RsbR&oldid=178765"