Difference between revisions of "RpoA"

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=References=
 
=References=
'''Additional publications:''' {{PubMed|20817769}}
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<pubmed>20084284 19726675 19580872 ,3093467,2496109,8635744,10675340,12486038,18643936, 12642660, 16249335, 16740936 ,22307755</pubmed>
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<pubmed>20084284 19726675 19580872 ,3093467,2496109,8635744,10675340,12486038,18643936, 12642660, 16249335, 16740936</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 17:24, 13 February 2012

Gene name rpoA
Synonyms
Essential yes PubMed
Product RNA polymerase alpha subunit
Function transcription
Interactions involving this protein in SubtInteract: RpoA
MW, pI 34 kDa, 4.593
Gene length, protein length 942 bp, 314 aa
Immediate neighbours rpsK, rplQ
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
RpoA context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

transcription, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU01430

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 alpha 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: 1Z3E (C-terminal domain, complex with Spx)
  • 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: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Additional publications: PubMed

Michiko M Nakano, Ann Lin, Cole S Zuber, Kate J Newberry, Richard G Brennan, Peter Zuber
Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit.
PLoS One: 2010, 5(1);e8664
[PubMed:20084284] [WorldCat.org] [DOI] (I e)

Andreas Licht, Sabine Brantl
The transcriptional repressor CcpN from Bacillus subtilis uses different repression mechanisms at different promoters.
J Biol Chem: 2009, 284(44);30032-8
[PubMed:19726675] [WorldCat.org] [DOI] (I p)

Valerie Lamour, Lars F Westblade, Elizabeth A Campbell, Seth A Darst
Crystal structure of the in vivo-assembled Bacillus subtilis Spx/RNA polymerase alpha subunit C-terminal domain complex.
J Struct Biol: 2009, 168(2);352-6
[PubMed:19580872] [WorldCat.org] [DOI] (I p)

Alexander Reder, Dirk Höper, Christin Weinberg, Ulf Gerth, Martin Fraunholz, Michael Hecker
The Spx paralogue MgsR (YqgZ) controls a subregulon within the general stress response of Bacillus subtilis.
Mol Microbiol: 2008, 69(5);1104-20
[PubMed:18643936] [WorldCat.org] [DOI] (I p)

Ying Zhang, Shunji Nakano, Soon-Yong Choi, Peter Zuber
Mutational analysis of the Bacillus subtilis RNA polymerase alpha C-terminal domain supports the interference model of Spx-dependent repression.
J Bacteriol: 2006, 188(12);4300-11
[PubMed:16740936] [WorldCat.org] [DOI] (P p)

Kate J Newberry, Shunji Nakano, Peter Zuber, Richard G Brennan
Crystal structure of the Bacillus subtilis anti-alpha, global transcriptional regulator, Spx, in complex with the alpha C-terminal domain of RNA polymerase.
Proc Natl Acad Sci U S A: 2005, 102(44);15839-44
[PubMed:16249335] [WorldCat.org] [DOI] (P p)

Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660] [WorldCat.org] [DOI] (P 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)

J W Suh, S A Boylan, S H Oh, C W Price
Genetic and transcriptional organization of the Bacillus subtilis spc-alpha region.
Gene: 1996, 169(1);17-23
[PubMed:8635744] [WorldCat.org] [DOI] (P p)

S A Boylan, J W Suh, S M Thomas, C W Price
Gene encoding the alpha core subunit of Bacillus subtilis RNA polymerase is cotranscribed with the genes for initiation factor 1 and ribosomal proteins B, S13, S11, and L17.
J Bacteriol: 1989, 171(5);2553-62
[PubMed:2496109] [WorldCat.org] [DOI] (P p)

J W Suh, S A Boylan, C W Price
Gene for the alpha subunit of Bacillus subtilis RNA polymerase maps in the ribosomal protein gene cluster.
J Bacteriol: 1986, 168(1);65-71
[PubMed:3093467] [WorldCat.org] [DOI] (P p)