Difference between revisions of "SigB"

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(Other publications)
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<pubmed> 11544224, 11532142, 11717291, 10482513, 10220166,22174379 </pubmed>
 
<pubmed> 11544224, 11532142, 11717291, 10482513, 10220166,22174379 </pubmed>
 
==Other publications==
 
==Other publications==
<pubmed>23407164,22511268,22210769 23524614  21979936  8655572,, 3123466, 10369900,3112122, 8468294,8458834, 13129942, 6784117, 12867438, 3100810, 8253681, 12486038, 8764398,3027048, 15342585,17575448, 17586624,,3016731,11902719,14651641,10503549,15205443,6405278, 10383961, 15805528 6790515 116131, 39767581 19948797 </pubmed>
+
<pubmed>23407164,22511268,22210769 23524614  21979936  8655572,, 3123466, 10369900,3112122, 8468294,8458834, 13129942, 6784117, 12867438, 3100810, 8253681, 12486038, 8764398,3027048, 15342585,17575448, 17586624,23934352, 3016731,11902719,14651641,10503549,15205443,6405278, 10383961, 15805528 6790515 116131, 39767581 19948797 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:36, 13 August 2013

Gene name sigB
Synonyms rpoF
Essential no
Product RNA polymerase sigma factor SigB
Function general stress response
Gene expression levels in SubtiExpress: sigB
Interactions involving this protein in SubtInteract: SigB
Metabolic function and regulation of this protein in SubtiPathways:
Stress, Murein recycling
MW, pI 29 kDa, 5.418
Gene length, protein length 792 bp, 264 aa
Immediate neighbours rsbW, rsbX
Sequences Protein DNA DNA_with_flanks
Genetic context
SigB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SigB expression.png















Categories containing this gene/protein

transcription, sigma factors and their control, general stress proteins (controlled by SigB)

This gene is a member of the following regulons

CcpA regulon, SigB regulon

The SigB regulon

The gene

Basic information

  • Locus tag: BSU04730

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: SigB subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Additional information:

Biological materials

  • Mutant: QB5344 (cat), available in the Stülke lab
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews


Control of SigB activity by protein-protein interactions

Oleg A Igoshin, Margaret S Brody, Chester W Price, Michael A Savageau
Distinctive topologies of partner-switching signaling networks correlate with their physiological roles.
J Mol Biol: 2007, 369(5);1333-52
[PubMed:17498739] [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)

Olivier Delumeau, Richard J Lewis, Michael D Yudkin
Protein-protein interactions that regulate the energy stress activation of sigma(B) in Bacillus subtilis.
J Bacteriol: 2002, 184(20);5583-9
[PubMed:12270815] [WorldCat.org] [DOI] (P p)

M S Brody, K Vijay, C W Price
Catalytic function of an alpha/beta hydrolase is required for energy stress activation of the sigma(B) transcription factor in Bacillus subtilis.
J Bacteriol: 2001, 183(21);6422-8
[PubMed:11591687] [WorldCat.org] [DOI] (P p)

C Eymann, M Hecker
Induction of sigma(B)-dependent general stress genes by amino acid starvation in a spo0H mutant of Bacillus subtilis.
FEMS Microbiol Lett: 2001, 199(2);221-7
[PubMed:11377871] [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)

U Voelker, A Voelker, B Maul, M Hecker, A Dufour, W G Haldenwang
Separate mechanisms activate sigma B of Bacillus subtilis in response to environmental and metabolic stresses.
J Bacteriol: 1995, 177(13);3771-80
[PubMed:7601843] [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)

A K Benson, W G Haldenwang
Bacillus subtilis sigma B is regulated by a binding protein (RsbW) that blocks its association with core RNA polymerase.
Proc Natl Acad Sci U S A: 1993, 90(6);2330-4
[PubMed:8460143] [WorldCat.org] [DOI] (P p)


Identification of the SigB regulon

Other publications