RpoE

• Description: RNA polymerase delta subunit
  
  

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 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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • closely associated to RNA polymerase (RpoA(2)-RpoB-RpoC) PubMed

• Localization:closely associated with RNA polymerase involved in transcribing both mRNA and rRNA operons PubMed

Database entries

• Structure: 2KRC PubMed

• UniProt: P12464

• KEGG entry: [3]

• E.C. number: 2.7.7.6

Expression and regulation

• Operon:
  • fadF-acdA-rpoE PubMed
  • rpoE PubMed

• Sigma factor:
  • fadF: SigA PubMed
  • rpoE: SigA PubMed

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

• Regulatory mechanism:
  • FadR: transcription repression PubMed

• Additional information:
  • present at equimolar levels with RNA polymerase PubMed

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

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)