Difference between revisions of "RpoA"

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* '''Additional information:'''
 
* '''Additional information:'''
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 
** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium): 3504 {{PubMed|24696501}}
 +
** number of protein molecules per cell (complex medium with amino acids, without glucose): 11832 {{PubMed|24696501}}
  
 
=Biological materials =
 
=Biological materials =

Revision as of 09:45, 17 April 2014

Gene name rpoA
Synonyms
Essential yes PubMed
Product RNA polymerase alpha subunit
Function transcription
Gene expression levels in SubtiExpress: rpoA
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
Sequences Protein DNA DNA_with_flanks
Genetic context
RpoA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RpoA expression.png















Categories containing this gene/protein

transcription, essential genes, most abundant proteins

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:
  • Modification:
  • 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:
    • belongs to the 100 most abundant proteins PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 3504 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 11832 PubMed

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

Reviews

Original publications

Andrea Wünsche, Elke Hammer, Maike Bartholomae, Uwe Völker, Andreas Burkovski, Gerald Seidel, Wolfgang Hillen
CcpA forms complexes with CodY and RpoA in Bacillus subtilis.
FEBS J: 2012, 279(12);2201-14
[PubMed:22512862] [WorldCat.org] [DOI] (I p)

Ann A Lin, Peter Zuber
Evidence that a single monomer of Spx can productively interact with RNA polymerase in Bacillus subtilis.
J Bacteriol: 2012, 194(7);1697-707
[PubMed:22307755] [WorldCat.org] [DOI] (I p)

Shu Ishikawa, Taku Oshima, Ken Kurokawa, Yoko Kusuya, Naotake Ogasawara
RNA polymerase trafficking in Bacillus subtilis cells.
J Bacteriol: 2010, 192(21);5778-87
[PubMed:20817769] [WorldCat.org] [DOI] (I p)

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)

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [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)