Difference between revisions of "RpoA"
| Line 41: | Line 41: | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[transcription]]}}, | {{SubtiWiki category|[[transcription]]}}, | ||
| − | {{SubtiWiki category|[[essential genes]]}} | + | {{SubtiWiki category|[[essential genes]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
| Line 79: | Line 80: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
| Line 115: | Line 116: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpoA_148931_149875_1 rpoA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=rpoA_148931_149875_1 rpoA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
| Line 123: | Line 124: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
| Line 146: | Line 148: | ||
<pubmed> 22210308 </pubmed> | <pubmed> 22210308 </pubmed> | ||
==Original publications== | ==Original publications== | ||
| − | + | <pubmed>20084284 19726675 19580872 ,3093467,2496109,8635744,10675340,12486038,18643936, 12642660, 16249335, 16740936 15378759 22512862,20817769,22307755</pubmed> | |
| − | <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 16:04, 5 March 2014
- 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
| |
Contents
Categories containing this gene/protein
transcription, essential genes, most abundant proteins
This gene is a member of the following regulons
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)
- UniProt: P20429
- KEGG entry: [2]
- E.C. number: 2.7.7.6
Additional information
Expression and regulation
- Operon:
- 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:
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)
