Difference between revisions of "RpoE"

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(References)
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** ''[[rpoE]]'' {{PubMed|10336502}}  
 
** ''[[rpoE]]'' {{PubMed|10336502}}  
  
* '''[[Sigma factor]]:'''  
+
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpoE_3812542_3813063_-1 rpoE] {{PubMed|22383849}}
 +
 
 +
* '''Sigma factor:'''  
 
** ''[[fadF]]'': [[SigA]] {{PubMed|17189250}}  
 
** ''[[fadF]]'': [[SigA]] {{PubMed|17189250}}  
 
** ''[[rpoE]]'': [[SigA]] {{PubMed|10336502}}  
 
** ''[[rpoE]]'': [[SigA]] {{PubMed|10336502}}  

Revision as of 08:29, 17 April 2012

Gene name rpoE
Synonyms
Essential no
Product RNA polymerase delta subunit
Function transcription
Interactions involving this protein in SubtInteract: RpoE
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid degradation
MW, pI 20 kDa, 3.654
Gene length, protein length 519 bp, 173 aa
Immediate neighbours pyrG, acdA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpoE context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

transcription

This gene is a member of the following regulons

FadR regulon

The gene

Basic information

  • Locus tag: BSU37160

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: rpoE family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • fadF: repressed in the absence of long-chain fatty acids (FadR) PubMed
  • Regulatory mechanism:

Biological materials

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

Labs working on this gene/protein

Arthur Aronson, Purdue University, West Lafayette, USA homepage

Your additional remarks

References

Additional publications: PubMed

Hiroshi Matsuoka, Kazutake Hirooka, Yasutaro Fujita
Organization and function of the YsiA regulon of Bacillus subtilis involved in fatty acid degradation.
J Biol Chem: 2007, 282(8);5180-94
[PubMed:17189250] [WorldCat.org] [DOI] (P p)

F J López de Saro, N Yoshikawa, J D Helmann
Expression, abundance, and RNA polymerase binding properties of the delta factor of Bacillus subtilis.
J Biol Chem: 1999, 274(22);15953-8
[PubMed:10336502] [WorldCat.org] [DOI] (P p)

F J López de Saro, A Y Woody, J D Helmann
Structural analysis of the Bacillus subtilis delta factor: a protein polyanion which displaces RNA from RNA polymerase.
J Mol Biol: 1995, 252(2);189-202
[PubMed:7545758] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
Pathway of promoter melting by Bacillus subtilis RNA polymerase at a stable RNA promoter: effects of temperature, delta protein, and sigma factor mutations.
Biochemistry: 1995, 34(26);8465-73
[PubMed:7599136] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
The delta subunit of Bacillus subtilis RNA polymerase. An allosteric effector of the initiation and core-recycling phases of transcription.
J Mol Biol: 1994, 239(1);1-14
[PubMed:7515111] [WorldCat.org] [DOI] (P p)

M Lampe, C Binnie, R Schmidt, R Losick
Cloned gene encoding the delta subunit of Bacillus subtilis RNA polymerase.
Gene: 1988, 67(1);13-9
[PubMed:2843435] [WorldCat.org] [DOI] (P p)

E I Hyde, M D Hilton, H R Whiteley
Interactions of Bacillus subtilis RNA polymerase with subunits determining the specificity of initiation. Sigma and delta peptides can bind simultaneously to core.
J Biol Chem: 1986, 261(35);16565-70
[PubMed:3097010] [WorldCat.org] (P p)

E C Achberger, H R Whiteley
The role of the delta peptide of the Bacillus subtilis RNA polymerase in promoter selection.
J Biol Chem: 1981, 256(14);7424-32
[PubMed:6788769] [WorldCat.org] (P p)