RpoA

• Description: RNA polymerase alpha subunit
  
  

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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• BsubCyc: BSU01430

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • RpoA-RpoB-RpoC PubMed
  • CcpN-RpoA PubMed
  • RpoA (C-terminal domain) -Spx PubMed
  • MgsR-RpoA PubMed
  • CcpA-RpoA PubMed
  • RpoA-CodY PubMed

• Localization:

Database entries

• BsubCyc: BSU01430

• Structure: 1Z3E (C-terminal domain, complex with Spx)

• UniProt: P20429

• KEGG entry: [2]

• E.C. number: 2.7.7.6

Expression and regulation

• Operon:

• Expression browser: rpoA PubMed

• Sigma factor:

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

• Regulatory mechanism:

• Additional information:
  • belongs to the 100 most abundant proteins 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:

References

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)