Difference between revisions of "RpoC"

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(Extended information on the protein)
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* '''Locus tag:''' BSU01080
 
* '''Locus tag:''' BSU01080
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[http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpoC_125562_129161_1 Expression]
  
 
===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===

Revision as of 12:16, 24 January 2012

Gene name rpoC
Synonyms
Essential yes PubMed
Product RNA polymerase beta' subunit
Function transcription
Interactions involving this protein in SubtInteract: RpoC
MW, pI 133 kDa, 8.863
Gene length, protein length 3597 bp, 1199 aa
Immediate neighbours rpoB, ybxF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpoC context.gif
This image was kindly provided by SubtiList





Categories containing this gene/protein

transcription, essential genes, membrane proteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01080

Expression

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1) (according to Swiss-Prot)
  • Protein family: RNA polymerase beta' chain 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

  • Structure:
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response 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

Additional publications: PubMed

Elecia B Johnston, Peter J Lewis, Renate Griffith
The interaction of Bacillus subtilis sigmaA with RNA polymerase.
Protein Sci: 2009, 18(11);2287-97
[PubMed:19735077] [WorldCat.org] [DOI] (I p)

Xiao Yang, Seeseei Molimau, Geoff P Doherty, Elecia B Johnston, Jon Marles-Wright, Rosalba Rothnagel, Ben Hankamer, Richard J Lewis, Peter J Lewis
The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA.
EMBO Rep: 2009, 10(9);997-1002
[PubMed:19680289] [WorldCat.org] [DOI] (I p)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Claudia Rollenhagen, Haike Antelmann, Janine Kirstein, Olivier Delumeau, Michael Hecker, Michael D Yudkin
Binding of sigma(A) and sigma(B) to core RNA polymerase after environmental stress in Bacillus subtilis.
J Bacteriol: 2003, 185(1);35-40
[PubMed:12486038] [WorldCat.org] [DOI] (P p)

P J Lewis, S D Thaker, J Errington
Compartmentalization of transcription and translation in Bacillus subtilis.
EMBO J: 2000, 19(4);710-8
[PubMed:10675340] [WorldCat.org] [DOI] (P p)

X Yang, C W Price
Streptolydigin resistance can be conferred by alterations to either the beta or beta' subunits of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(41);23930-3
[PubMed:7592585] [WorldCat.org] [DOI] (P p)

K J Boor, M L Duncan, C W Price
Genetic and transcriptional organization of the region encoding the beta subunit of Bacillus subtilis RNA polymerase.
J Biol Chem: 1995, 270(35);20329-36
[PubMed:7657605] [WorldCat.org] [DOI] (P p)