Difference between revisions of "RsbT"

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* '''Description:''' PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome <br/><br/>
+
* '''Description:''' PP2C activator, protein serine kinase, phosphorylates [[RsbS]], part of the stressosome <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || PP2C activator, protein serine kinase
 
|style="background:#ABCDEF;" align="center"| '''Product''' || PP2C activator, protein serine kinase
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Function''' || control of SigB activity
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|style="background:#ABCDEF;" align="center"|'''Function''' || control of [[SigB]] activity
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/stress_response.html Stress]'''
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* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed]
 
* '''[[Sigma factor]]:''' [[SigA]] [http://www.ncbi.nlm.nih.gov/sites/entrez/8002610 PubMed]
  
* '''Regulation:'''  
+
* '''Regulation:''' constitutively expressed {{PubMed|20019076}}
  
 
* '''Regulatory mechanism:'''  
 
* '''Regulatory mechanism:'''  
  
 
* '''Additional information:'''
 
* '''Additional information:'''
 +
** [[RsbT]] is synthesized at the same rate as [[RsbRA]] and [[RsbS]], however, the [[RsbT]] level in growing ''B. subtilis'' is only 10% that of [[RsbRA]], suggesting that the protein is unstable {{PubMed|20019076}}.
  
 
=Biological materials =
 
=Biological materials =
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<pubmed>19704888 16319496  </pubmed>
 
<pubmed>19704888 16319496  </pubmed>
 
==Original Articles==
 
==Original Articles==
<pubmed>8682789,8002610,8682769,9658013,17303566, 9786195,15090521,10781545, 15583165, 8824586, 10329124,16321960,8808936,15312768,11244072,15342582,,12499568, 12950928, 16321960, 8955331,  18832644</pubmed>
+
<pubmed>8682789,8002610,8682769,9658013,17303566, 9786195,15090521,10781545, 15583165, 8824586, 10329124,16321960,8808936,15312768,11244072,15342582,20019076, 12499568, 12950928, 16321960, 8955331,  18832644</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 11:02, 19 December 2009

  • Description: PP2C activator, protein serine kinase, phosphorylates RsbS, part of the stressosome

Gene name rsbT
Synonyms ycxT
Essential no
Product PP2C activator, protein serine kinase
Function control of SigB activity
Metabolic function and regulation of this protein in SubtiPathways:
Stress
MW, pI 14 kDa, 6.587
Gene length, protein length 399 bp, 133 aa
Immediate neighbours rsbS, rsbU
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RsbT context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU04690

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + a protein = ADP + a phosphoprotein (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

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:
    • RsbT is synthesized at the same rate as RsbRA and RsbS, however, the RsbT level in growing B. subtilis is only 10% that of RsbRA, suggesting that the protein is unstable PubMed.

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

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)

Steven W Hardwick, Jan Pané-Farré, Olivier Delumeau, Jon Marles-Wright, James W Murray, Michael Hecker, Richard J Lewis
Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.
J Biol Chem: 2007, 282(15);11562-72
[PubMed:17303566] [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)

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)

Robyn L Woodbury, Tingqiu Luo, Lindsay Grant, W G Haldenwang
Mutational analysis of RsbT, an activator of the Bacillus subtilis stress response transcription factor, sigmaB.
J Bacteriol: 2004, 186(9);2789-97
[PubMed:15090521] [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)

Sujit Dutta, Richard J Lewis
Crystallization and preliminary crystallographic analysis of the kinase-recruitment domain of the PP2C-type phosphatase RsbU.
Acta Crystallogr D Biol Crystallogr: 2003, 59(Pt 1);191-3
[PubMed:12499568] [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)

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)

N Smirnova, J Scott, U Voelker, W G Haldenwang
Isolation and characterization of Bacillus subtilis sigB operon mutations that suppress the loss of the negative regulator RsbX.
J Bacteriol: 1998, 180(14);3671-80
[PubMed:9658013] [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)